Name: tandem mass spectrometry for biomolecule analysis
Uploaded: 2023-04-30T06:31:22.000Z
Duration: 7 min 9 s
Channel: JoVE

K12 Standards

Next Generation Science Standards

High School

Physical Science

waves-and-their-applications-in-technologies-for-information-transfer

Waves and Their Applications in Technologies for Information Transfer

HS-PS4-5

Tandem Mass Spectrometry

spectrometría de masas de tándem

En spectrometry total en tándem biomoléculas de interés es aislada de una muestra biológica y luego se fragmentó en múltiples subunidades con el fin de ayudar a elucidar su composición y secuencia. Esto se logra con espectrómetros de masas en serie. El primer espectrómetro ioniza una muestra y el filtro de iones de una masa específica para cargar cociente. Filtrado iones entonces son fragmentados y pasa a un segundo espectrómetro de masas donde se analizan los fragmentos.
Este video presenta los principios de la espectrometría total en tándem, incluyendo métodos de selección y disociación de ratio de masa. También se muestra es un procedimiento general para el análisis de un compuesto bioquímico usando spectrometry total en tándem con la disociación colisión-inducida. La sección de aplicaciones cubre reacción selección supervisión, determinación de las modificaciones post traducción en proteína y la detección de los niveles de tacrolimus en sangre.
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Enlaces de espectrometría de masas tándem juntos múltiples etapas de espectrometría de masas primero aislar una biomolécula y luego determinan los aspectos de su composición química. Biomoléculas tienen estructuras grandes y complejas, lo que hace difícil determinar su composición molecular. Espectrometría de masas tándem selecciona una molécula de interés que más tarde se fragmentó en múltiples subunidades, que pueden ayudar a elucidar su identificación y secuencia. Este video le mostrará los conceptos de la espectrometría total en tándem, un procedimiento general y algunas de sus aplicaciones en bioquímica.
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Espectrometría de masas tándem comienza como un típico instrumento masa Especificaciones: con una fuente de iones, que convierte la muestra en iones y un analizador de masas, que separa los iones basados en su relación masa / carga. Un analizador de masa común, el cuadrupolo, sólo permite los iones con una relación específica, mientras que los otros crash en las barras del aparato. Las especies permitidas, llamado ion del precursor, es las biomoléculas de interés. El ion se mueve en una celda de colisión, por lo general otro quadrupole, donde energía se aplica a los iones en un patrón predecible.
Estos fragmentos se trasladan a otro analizador de la masa, como un tiempo de vuelo, que separa a estos "iones del producto". Los iones producto son enviados al detector, como un instrumento MS normal. En el caso de una proteína desconocida, el espectro resultante contiene numerosos fragmentos solapados, haciendo difícil generar una secuencia completa definitiva de las biomoléculas. Sin embargo, el patrón espectral es único para una determinada proteína. Software de análisis compara el espectro a una base de datos de secuencias de péptidos conocidos, elucidar la proteína desconocida de los fragmentos solapados.
Dependiendo de la muestra y el grado deseado de fragmentación, varios métodos de fragmentación son posibles. Patrones de fragmentación dependen de cómo la energía se transfiere, su cantidad, y cómo se distribuye a través del ion precursor. Energía puede transferirse por medio de radiación y partículas neutras y electrones. Sobre todo utilizando átomos neutrales, un proceso llamado disociación colisión-inducida o CID, hiende en el enlace peptídico entre los aminoácidos, ideales para su identificación.
Ahora que se han cubierto los fundamentos de la técnica, echemos un vistazo a spectrometry total en tándem CID siendo utilizado para el estudio de un componente de los sobres de la célula bacteriana.
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Como con todos los experimentos espectrometría de masa, el primer paso es ionizar la muestra. Para biomoléculas, esto normalmente se hace con desorción láser de matriz asistida o de ionización por electrospray. La señal de ion precursor entonces se optimiza mediante la regulación de la óptica del ion. Una vez hecho esto, el objetivo es aislado y se elige el método de fragmentación, como el CID.
La fuerza de un voltaje aplicado, que acelera el ion precursor en la celda de colisión, afecta el grado de fragmentación. Esta tensión se incrementa hasta que el precursor es aproximadamente 10% abundancia en comparación con el ion de producto más alto. Múltiples espectros son adquiridos y promedio hasta que se logra una relación señal a ruido suficiente. El número de exploraciones es necesitada depende de la intensidad de la señal del ión precursor original y puede variar de 3 a 300.
Analito en este ejemplo, el lípido A de Escherichia coli K-12, tenía 19 fragmentos principales después del CID. Estructura general de lípido s es bien conocida, que software reconstruir la composición específica de la muestra.
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Ahora que hemos mirado el procedimiento, Veamos algunas de las maneras de espectrometría de masas tándem es utilizado en bioquímica.
Un modo común de la exploración en espectrometría de masas tándem es reacción seleccionada supervisión o SRM. En SRM, ambos analizadores de masas están fijados a una relación de masa de la carga seleccionada, centrándose en los iones precursores y productos específicos. Debido a alto grado de sensibilidad de SRM, los espectros de niveles de péptido de concentración conocida pueden ser utilizados y comparada con la de las muestras desconocidas, permitiendo que las proteínas de interés para ser cuantificada.
Las proteínas son modificadas comúnmente después de traducción, normalmente mediante la adición de grupos funcionales como los grupos metilo, grupos fosfato y azúcares, conocidos como glycans. Estos son importantes en procesos de señalización de células elucidar cómo las células se comunican uno con el otro. Como espectrometría de masas tándem fragmentos de las proteínas en componentes más pequeños, es posible determinar la ubicación de la PTM el fragmento específico o incluso un aminoácido. Algunas modificaciones, como la acetilación y trimetilación, son difíciles de distinguir por la masa sola, para que la separación cromatográfica se realiza antes de la espectrometría de masas.
Muchos analitos en sangre del paciente se encuentran en concentraciones por debajo del límite de detección por espectrometría de masas típico. Otra ventaja de SRM es que Descartes todos sino un ion del producto, aumentar la sensibilidad y mejorar el límite de detección inferior en hasta 100 veces. En este ejemplo, el fármaco inmunosupresor tacrolimus, pudo detectarse a nivel de 1 ng/mL.
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Sólo has visto video de Zeus en spectrometry total en tándem. Este video describe la teoría del instrumento, fue un procedimiento general y explicó algunas de las maneras que la técnica está siendo utilizada actualmente. ¡Gracias por ver!
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Spectrometría de masas de tándem

In tandem mass spectrometry a biomolecule of interest is isolated from a biological sample, and then fragmented into multiple subunits in order to help ...

La espectrometría de masas en tándem vincula múltiples etapas de espectrometría de masas para aislar primero una biomolécula y luego determinar aspectos de su composición química. Las biomoléculas tienen estructuras grandes y complejas, lo que dificulta la determinación de su composición molecular. La espectrometría de masas en tándem selecciona una molécula de interés que luego se fragmenta en múltiples subunidades, lo que puede ayudar a dilucidar su identificación y secuencia. Este video mostrará los conceptos de la espectrometría de masas en tándem, un procedimiento general y algunos de sus usos en bioquímica. La espectrometría de masas en tándem comienza como un instrumento típico de espectrometría de masas: con una fuente de iones, que convierte la muestra en iones, y un analizador de masas, que separa los iones en función de su relación masa-carga. Un analizador de masas común, el cuadrupolo, solo permite el paso de iones con una relación específica, mientras que los otros chocan contra las varillas del aparato. La especie permitida a través de ella, llamada ion precursor, es la biomolécula de interés. El ion se mueve a una celda de colisión, generalmente otro cuadrupolo, donde se aplica energía para fragmentar el ion en un patrón predecible. Estos fragmentos se mueven a otro analizador de masas, como un tiempo de vuelo, que separa estos "iones producto". A continuación, los iones producto se envían al detector, como en un instrumento MS normal. En el caso de una proteína desconocida, el espectro resultante contiene numerosos fragmentos superpuestos, lo que dificulta la generación de una secuencia completa y definitiva de la biomolécula. Sin embargo, el patrón espectral es único para una proteína determinada. El software de análisis compara el espectro con una base de datos de secuencias de péptidos conocidas, dilucidando la proteína desconocida a partir de los fragmentos superpuestos. Dependiendo de la muestra y del grado de fragmentación deseado, son posibles varios métodos de fragmentación. Los patrones de fragmentación dependen de cómo se transfiere la energía, su cantidad y cómo se distribuye a través del ion precursor. La energía se puede transferir a través de partículas neutras, radiación o electrones. El uso de átomos neutros, un proceso llamado disociación inducida por colisión o CID, se escinde principalmente en el enlace peptídico entre los aminoácidos, ideal para su identificación. Ahora que se han cubierto los conceptos básicos de la técnica, echemos un vistazo a la espectrometría de masas en tándem CID que se utiliza para estudiar un componente de las envolturas de células bacterianas. Como en todos los experimentos de espectrometría de masas, el primer paso es ionizar la muestra. En el caso de las biomoléculas, esto se suele hacer con desorción láser asistida por matriz o ionización por electropulverización. A continuación, la señal de iones precursores se optimiza mediante el ajuste de la óptica de iones. Una vez hecho esto, se aísla el objetivo y se elige el método de fragmentación, como CID. La fuerza de un voltaje aplicado, que acelera el ion precursor en la celda de colisión, afecta el grado de fragmentación. Este voltaje se incrementa hasta que el precursor tiene aproximadamente un 10% de abundancia en comparación con el ion producto más alto. Se adquieren múltiples espectros y se promedian hasta que se logra una relación señal-ruido suficiente. El número de exploraciones necesarias depende de la intensidad de la señal del ion precursor original y puede oscilar entre 3 y 300. El analito de este ejemplo, el lípido A de Escherichia coli K-12, tenía 19 fragmentos principales después de la CID. La estructura general del lípido A es bien conocida, lo que permite al software reconstruir la composición específica de la muestra. Ahora que hemos visto el procedimiento, veamos algunas de las formas en que se utiliza la espectrometría de masas en tándem en bioquímica. Un modo de escaneo común en la espectrometría de masas en tándem es el monitoreo de reacción seleccionado, o SRM. En SRM, ambos analizadores de masas se fijan a una relación masa-carga seleccionada, centrándose en precursores e iones de productos específicos. Debido al alto grado de sensibilidad del SRM, se pueden utilizar y comparar los espectros de los patrones peptídicos de concentración conocida con los de las muestras desconocidas, lo que permite cuantificar las proteínas de interés. Las proteínas se modifican comúnmente después de la traducción, generalmente mediante la adición de grupos funcionales como grupos metilo, grupos fosfato o azúcares, conocidos como glicanos. Estos son importantes en los procesos de señalización celular, dilucidando cómo las células se comunican entre sí. Debido a que la espectrometría de masas en tándem fragmenta las proteínas en componentes más pequeños, es posible determinar la ubicación del PTM en el fragmento específico o incluso en un aminoácido. Algunas modificaciones, como la acetilación y la trimetilación, son difíciles de diferenciar solo por la masa, por lo que la separación cromatográfica se realiza antes de la espectrometría de masas. Muchos analitos en la sangre del paciente se encuentran en concentraciones por debajo del límite de detección para la espectrometría de masas típica. Otra ventaja de SRM es que descarta todos los iones del producto excepto uno, lo que aumenta la sensibilidad y mejora el límite inferior de detección hasta 100 veces. En este ejemplo, el fármaco inmunosupresor, tacrolimus, podría detectarse a niveles de 1 ng/mL. Acabas de ver el vídeo de JoVE sobre la espectrometría de masas en tándem. Este video describió la teoría del instrumento, repasó un procedimiento general y explicó algunas de las formas en que la técnica se utiliza actualmente. ¡Gracias por mirar!

Education

Educación

JoVE Science Education

Chemistry

Química

Biochemistry

Bioquímica

tandem mass spectrometry for biomolecule analysis

Tandem mass spectrometry is used to isolate a biomolecule and break it into smaller pieces so its makeup can be studied. Because biomolecules often have large, complex structures, it can be hard to identify their molecular composition and sequence from a single measurement. By linking mass spectrometers in series, the technique first selects one ion and then analyzes the fragments it produces.

The process starts with an ion source that converts the sample into ions. A mass analyzer then separates those ions by their mass-to-charge ratio, also called m/z. In a quadrupole, only ions with a chosen m/z pass through, while the others strike the rods. The selected precursor ion is the molecule of interest.

That ion moves into a collision cell, often another quadrupole, where energy breaks it apart in a predictable pattern. The fragments, called product ions, then enter a second mass analyzer such as a time-of-flight instrument. After separation, the detector records the signals. For an unknown protein, the spectrum can contain many overlapping fragments, but the pattern is still unique. Software can compare it with a database of known peptide sequences to identify the protein.

Different fragmentation methods can be used depending on the sample and the level of detail needed. The outcome depends on how energy is transferred, how much is transferred, and how it spreads through the precursor ion. Energy may come from neutral particles, radiation, or electrons. With collision-induced dissociation, or CID, neutral atoms are used and the peptide bond between amino acids is usually cleaved, which helps with identification.

CID tandem mass spectrometry can also be used to study a bacterial cell envelope component. In that example, the sample is first ionized by matrix assisted laser desorption or electrospray ionization. The precursor ion signal is then optimized by tuning the ion optics, and the target is isolated before CID is selected. The applied voltage controls how much fragmentation occurs, and it is increased until the precursor is about 10% as abundant as the highest product ion. Multiple scans are collected and averaged until the signal-to-noise ratio is strong enough. For lipid A from Escherichia coli K-12, 19 major fragments were observed, and its known structure let software reconstruct the composition.

Tandem mass spectrometry is also used for selected reaction monitoring, or SRM. In SRM, both mass analyzers are fixed to a chosen m/z so the instrument focuses on specific precursor and product ions. This high sensitivity makes it useful for comparing peptide standards of known concentration with unknown samples to measure proteins of interest. The method is also helpful for detecting post-translational modifications, or PTMs, such as methyl groups, phosphate groups, and sugars called glycans, which play roles in cell signaling. Because the sample is broken into smaller pieces, the modification can sometimes be placed on a specific fragment or amino acid.

Some PTMs, such as acetylation and trimethylation, are hard to tell apart by mass alone, so chromatographic separation is done before mass spectrometry. SRM can also improve detection of very low-level compounds in blood. By removing all but one product ion, it can raise sensitivity and lower the detection limit by up to 100 fold. In the example shown, the immunosuppressant tacrolimus was detected at 1 ng/mL.

Tandem Mass Spectrometry for Biomolecule Analysis

tandem-mass-spectrometry-for-biomolecule-analysis

dialysis: diffusion based separation

Dialysis for Buffer Exchange in Biochemistry

Dialysis is a common biochemistry technique for buffer exchange and desalting. It separates molecules by diffusion through a semipermeable membrane, which lets small molecules pass while holding larger biomolecules inside the sample. The membrane is the key part of the setup. Its pores create a molecular weight cutoff, so a membrane such as a 10 kDa membrane usually keeps molecules larger than 10 kilodaltons inside. This cutoff is not exact, because membranes have a range of pore sizes.

enzyme assays and kinetics

Measuring Enzyme Reaction Rates

Enzyme reaction rates can be measured with assays that track how substrate or product levels change over time. Enzymes are proteins, or sometimes RNAs, that speed up chemical reactions by lowering the activation energy needed to start them. They act on a specific substrate and help form a product that supports life processes. Enzymatic reactions are often described in three steps. First, the substrate binds to the enzyme active site and forms an enzyme-substrate complex. That complex can fall...

maldi-tof mass spectrometry

How MALDI-TOF Reads Biomolecules

MALDI-TOF mass spectrometry reads biomolecules by using a laser, a matrix, and a time-of-flight analyzer. MALDI, or matrix-assisted laser desorption ionization, helps fragile molecules keep their structure while they are moved into the mass analyzer. The analyzer then separates compounds based on size and charge. In MALDI, the sample is mixed into a matrix, usually an organic compound with aromatic and conjugated double bonds. A laser pulse strikes the spot, and the matrix absorbs most of the...

tandem mass spectrometry

Tandem mass spectrometry is used to isolate a biomolecule and break it into smaller pieces so its makeup can be studied. Because biomolecules often have large, complex structures, it can be hard to identify their molecular composition and sequence from a single measurement. By linking mass spectrometers in series, the technique first selects one ion and then analyzes the fragments it produces. The process starts with an ion source that converts the sample into ions. A mass analyzer then...

protein crystallization

Protein Crystals for Structure Analysis

Protein crystals help scientists study protein structure and function. A crystal is a solid lattice made from purified protein molecules. These crystals are useful in structural biology because they reveal details that methods like mass spectrometry and SDS-PAGE cannot show on their own. Protein crystallization is paired with recombinant protein expression and x-ray diffraction to support this work. The process starts with a large amount of very pure protein. Researchers often make that...

chromatography-based biomolecule purification methods

chromatography-based-biomolecule-purification-methods

Protein Purification with SEC and IMAC

Protein purification with size-exclusion chromatography and affinity chromatography helps isolate biomolecules from complex mixtures. These methods are common in biochemistry because purified samples are needed before a biomolecule’s properties and activity can be studied. The video focuses on the principles behind size-exclusion chromatography, affinity chromatography, and immobilized metal affinity chromatography, or IMAC. Size-exclusion chromatography, or SEC, separates molecules by size. A...

two-dimensional gel electrophoresis

Protein Mapping with 2D Gel Electrophoresis

Protein mapping with 2D gel electrophoresis separates complex protein mixtures across two steps. The method combines isoelectric focusing, or IEF, with sodium dodecyl sulfate polyacrylamide gel electrophoresis, or SDS-PAGE. Together, these methods can resolve thousands of biomolecules from a single sample by their isoelectric point and molecular weight. The first dimension is IEF. Each protein has an isoelectric point, or pI, which is the pH where its net charge is zero. Proteins are loaded...

metabolic labeling

Tracking Cell Chemistry with Metabolic Labels

Metabolic labeling tracks cell chemistry by using chemical analogs that cells take up and build into biomolecules. These labels help scientists follow biochemical changes and modifications inside cells. The labeled products can then be studied with tools such as SDS-PAGE and NMR to learn more about metabolic pathways. Several labeling strategies are shown here. Isotopic labeling uses analogs that match the natural molecule but contain uncommon isotopes, such as carbon-13 and nitrogen-15 in an...

electrophoretic mobility shift assay (emsa)

electrophoretic-mobility-shift-assay-emsa

Detecting Protein-DNA Binding by EMSA

Electrophoretic mobility shift assay, or EMSA, is a biochemical method used to detect binding between proteins and nucleic acids. It is also called a gel shift assay. The test compares how a labeled nucleic acid moves through a gel before and after it binds a protein. EMSA is used to see whether a specific protein binds to a specific nucleic acid. First, the nucleic acid is labeled to make a probe. The transcript describes radioactive phosphorus-32 as a common label. The probe is then mixed...

photometric protein determination

Measuring Protein Concentration with Absorbance

Measuring protein concentration with absorbance is a key step in many biochemical assays. Photometric methods use the fact that samples with more light-absorbing material transmit less light. Because concentration and absorption are directly related, this makes it possible to measure an unknown sample. The core idea comes from the Beer-Lambert Law. This law states that the concentration of a light-absorbing species is proportional to its absorbance. The video also introduces the Bradford assay...

density gradient ultracentrifugation

Sucrose Gradient Separation in an Ultracentrifuge

Sucrose gradient separation in an ultracentrifuge is a lab method for isolating cell parts and biomolecules. It uses differences in density to make particles sink or rise in a liquid. A high-speed ultracentrifuge speeds up this process so components can be separated without destroying them. The basic idea starts with a suspension, which is particles mixed in a liquid solvent. Particles that are denser than the solvent sediment, while less dense particles float. A rotor inside the...

co-immunoprecipitation and pull-down assays

co-immunoprecipitation-and-pull-down-assays

Protein Interaction Capture Methods in Cells

Co-immunoprecipitation and pull-down assays are laboratory methods used to capture stable protein-protein interactions. Protein-protein interactions help control many biological functions, but many of them have not yet been identified. These assays are related to immunoprecipitation, which isolates a target protein from a mixed sample using an antibody. In co-immunoprecipitation, or CoIP, an antibody binds the target protein, and that protein is already attached to another protein that the...

reconstitution of membrane proteins

Membrane Proteins in Liposome Models

Membrane proteins can be moved into liposome models so their function can be studied outside a cell. Reconstitution means restoring an isolated biomolecule to a working form. For membrane proteins, that usually means placing a purified protein into an artificial lipid membrane. Cell membranes are made mainly of phospholipids and membrane proteins. The phospholipids form a bilayer with hydrophilic phosphate heads facing water and hydrophobic fatty acid tails facing inward. Some membrane...

f&#246;rster resonance energy transfer (fret)

FRET as a Molecular Ruler in Cells

Föster resonance energy transfer, or FRET, is a way to study close-range biochemical interactions using light-emitting molecules. A donor fluorophore can pass energy to an acceptor fluorophore when their emission and absorption spectra overlap. This transfer happens only when the pair is very close together, usually within 10 nm. Because FRET depends on distance, it is often called a molecular or spectroscopic ruler. The strength of the signal is measured as FRET efficiency, which describes...

surface plasmon resonance (spr)

SPR Biosensors for Tracking Binding Kinetics

Surface plasmon resonance, or SPR, is a way to track biomolecular binding on a label-free biosensor. It is used to measure molecular affinity, kinetics, specificity, and concentration. The method works with a thin metal layer on a prism, where changes in reflected light reveal interactions in real time. SPR sensors use a thin layer of a noble metal on the face of a prism. Light is reflected from the prism-metal interface into a photodetector. At one specific angle, called the surface plasmon...

biochemistry

Esta colección presenta varios métodos de purificación comúnmente usados, como la cromatografía de afinidad y métodos analíticos, como MALDI-TOF. Además, los videos muestran métodos para evaluar la interacción y la función de diversas biomoléculas como en la coprecipitación y el etiquetado metabólico.

Learn how tandem mass spectrometry isolates biomolecules, fragments them, and helps detect proteins, PTMs, and low-level drugs in blood.

Tandem Mass Spectrometry for Biomolecule Analysis | JoVE K12

new-york-state-science-learning-standards

New York State Science Learning Standards

HS. Waves and Electromagnetic Radiation

HS-PS4-5.

Life Science

matter-and-energy-in-organisms-and-ecosystems

Matter and Energy in Organisms and Ecosystems

HS-LS1-6.

Overview

Principles of Tandem Mass Spectrometry

Instrumental Operation

Applications

Summary

Travelling Waves

A wave is a disturbance that propagates from its source, repeating itself periodically, and is typically associated with simple harmonic motion. ...

Wave Parameters

The simplest mechanical waves are associated with simple harmonic motion and repeat themselves for several cycles. These simple harmonic waves can be ...

Equations of Wave Motion

Mathematically, the motion of a wave can be studied using a wavefunction. Consider a string oscillating up and down in simple harmonic motion, having a ...

Graphing the Wave Function

Consider the wave equation for a sinusoidal wave moving in the positive x-direction. The wave equation is a function of both position and time. From the ...

/files/media/science-education/science-education-thumbs/14721.jpg

Velocity and Acceleration of a Wave

A wave propagates through a medium with a constant speed, known as a wave velocity. It is different from the speed of the particles of the medium, which ...

Speed of a Transverse Wave

The speed of a wave depends on the characteristics of the medium. For example, in the case of a guitar, the strings vibrate to produce the sound. The ...

/files/media/science-education/science-education-thumbs/14722.jpg

Kinetic and Potential Energy of a Wave

All forms of waves carry energy; this is directly visualized in nature. For instance, the waves of earthquakes are so intense that they can shake huge ...

Energy and Power of a Wave

The total energy associated with a wavelength is the sum of the potential energy and the kinetic energy. The average rate of energy transfer associated ...

Propagation of Waves

When a wave propagates from one medium to another, part of it may get reflected in the first medium, and part of it may get transmitted to the second ...

Sound Waves

Sound waves can be thought of as fluctuations in the pressure of a medium through which they propagate. Since the pressure also makes the medium&#39;s ...

Sound as Pressure Waves

Sound waves, which are longitudinal waves, can be modeled as the displacement amplitude varying as a function of the spatial and temporal coordinates. As ...

/files/media/science-education/science-education-thumbs/14724.jpg

Speed of Sound in Solids and Liquids

Most solids and liquids are incompressible&#8212;their densities remain constant throughout. In the presence of an external force, the molecules tend to ...

Speed of Sound in Gases

The speed of sound in a gaseous medium depends on various factors. Since gases constitute molecules that are free to move, they are highly compressible. ...

Doppler Effect - I

The Doppler effect and Doppler shift were named after the Austrian physicist and mathematician Christian Johann Doppler in 1842, who conducted experiments ...

Doppler Effect - II

The Doppler effect has several practical, real-world applications. For instance, meteorologists use Doppler radars to interpret weather events based on ...

Shock Waves

While deriving the Doppler formula for the observed frequency of a sound wave, it is assumed that the speed of sound in the medium is greater than the ...

Echo

The human ear cannot distinguish between two sources of sound if they happen to reach within a specific time interval, typically 0.1 seconds apart. More ...

/files/media/science-education/science-education-thumbs/14729.jpg

Electromagnetic Waves

James Clerk Maxwell formulated a single theory combining all the electric and magnetic effects scientists knew during that time, calling the phenomena his ...

Generating Electromagnetic Radiations

The German physicist Heinrich Hertz (1857&#8211;1894) was the first to generate and detect certain types of electromagnetic waves in the laboratory. ...

Electromagnetic Wave Equation

Maxwell&#39;s equations for electromagnetic fields are related to source charges, either static or moving. These fields act on a test charge, whose ...

propagation-speed-of-electromagnetic-waves

Propagation Speed of Electromagnetic Waves

Electromagnetic waves are consistent with Ampere&#39;s law. Assuming there is no conduction current Ampere&#39;s law is given as:


Consider a plane ...

Electromagnetic Waves in Matter

Electromagnetic waves can travel in the vacuum as well as in matter. For example light, which is an electromagnetic wave, can travel through air, water, ...

Energy Carried By Electromagnetic Waves

Anyone who has used a microwave oven knows there is energy in electromagnetic waves. Sometimes, this energy is obvious, such as in the summer sun&#39;s ...

The Wave Nature of Light

The nature of light has been a subject of inquiry since antiquity. In the seventeenth century, Isaac Newton performed experiments with lenses and prisms ...

Use mathematical representations to support a claim regarding relationships among the frequency, wavelength, and speed of waves traveling in various media. [Clarification Statement: Examples of data could include electromagnetic radiation traveling in a vacuum and glass, sound waves traveling through air and water, and seismic waves traveling through the earth.] [Assessment Boundary: Assessment is limited to algebraic relationships and describing those relationships qualitatively.]

HS-PS4-1

The Electromagnetic Spectrum

Electromagnetic waves are categorized according to their wavelengths and frequencies, giving the electromagnetic spectrum. These waves are classified as ...

Classification of Signals

Signals are categorized as Continuous-time or discrete-time, Periodic or aperiodic, Analog or digital, and Causal or noncausal.
A continuous-time signal ...

Discrete Fourier Transform

Consider a vibration sensor that continuously captures data in the form of a continuous time-dependent signal.
However, in reality, the sensor can only ...

Discrete-Time Fourier Series

The Discrete-Time Fourier Series is a counterpart to the Fourier-series expansion of continuous-time periodic signals.
Calculating the expansion ...

Sampling Theorem

Consider the continuous-time signal x(t), and a train of impulses where Ts,&#xA0; is the sampling interval, and fs, is the sampling frequency.
Multiplying ...

Properties of Fourier Transform I

In radio broadcasting, Fourier Transform properties are applied in simultaneous multi-channel transmission, adjusting audio clip speeds, live broadcast ...

Signal and System

Signals are sets of data or information.
One-dimensional signals include single-variable functions, such as the variations in air pressure over time in ...

Methods of Documentation VII: EMR

Electronic Medical Records (EMRs) primarily center around electronically documenting patients&#39; health information within a single healthcare ...

Fast Fourier Transform

The Fast Fourier Transform, FFT, is a computational algorithm for calculating the Discrete Fourier Transform by breaking the calculations into smaller, ...

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Reconstruction of Signal using Interpolation

Consider a continuous signal and its sampled counterpart with a sampling period T.
Applying a zero-order hold to the sampled signal results in a piecewise ...

Downsampling

Consider a sampled sequence with zero values between sampling instants. Replace it by taking every N-th value of the sampled sequence.
The original and ...

Design Example

An engineer designs a circuit for a speaker system with a 2 kHz crossover frequency requirement, considering the speaker&#39;s resistance of 8 ohms.
The ...

Upsampling

Consider a decimated signal with a reduced frequency range due to its lower sampling rate.
Insert zeros between each sample to upsample, that introduces ...

Properties of DTFT I

Consider two discrete-time signals, each with their respective Discrete-Time Fourier Transforms DTFTs.
The signals are first multiplied by constants a and ...

Relation of DFT to z-Transform

The Discrete Fourier Transform (DFT) analyzes the frequency content of discrete-time signals.
It maps the N-sampled discrete time-domain sequence to its ...

Feedback control systems

Feedback control systems are categorized as linear or nonlinear, time-varying or time-invariant, and classified by signal types as continuous or ...

Properties of the z-Transform I

Certain properties provide a solid foundation for analyzing discrete-time systems using the Z-transform.
Considering two discrete-time signals, the ...

Magnetic Resonance Imaging

Magnetic resonance imaging (MRI) is a noninvasive medical imaging technique based on a phenomenon of nuclear physics discovered in the 1930s, in which ...

Evaluate questions about the advantages of using digital transmission and storage of information. [Clarification Statement: Examples of advantages could include that digital information is stable because it can be stored reliably in computer memory, transferred easily, and copied and shared rapidly. Disadvantages could include issues of easy deletion, security, and theft.]

HS-PS4-2

Interference and Superposition of Waves

When two waves of the same nature occur in the same region simultaneously, they result in interference. Interference of waves implies that the net effect ...

Sound Waves: Interference

Sound waves can be modeled either as longitudinal waves, wherein the molecules of the medium oscillate around an equilibrium position, or as pressure ...

Interference: Path Lengths

Consider two sources of sound, that may or may not be in phase, emitting waves at a single frequency, and consider the frequencies to be the same.
Two ...

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concept-of-resonance-and-its-characteristics

Concept of Resonance and its Characteristics

If a driven oscillator needs to resonate at a specific frequency, then very light damping is required. An example of light damping includes playing piano ...

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Sound Waves: Resonance

Resonance is produced depending on the boundary conditions imposed on a wave. Resonance can be produced in a string under tension with symmetrical ...

Reflection of Waves

When a wave travels from one medium to another, it gets reflected at the boundary of the second medium. A common example of this is when a person yells at ...

Standing Waves

Sometimes waves do not seem to move; rather, they just vibrate in place. Unmoving waves can be seen on the surface of a glass of milk kept in a ...

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Modes of Standing Waves - I

A close look at earthquakes provides evidence for the conditions appropriate for resonance, standing waves, and constructive and destructive interference. ...

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Evaluate the claims, evidence, and reasoning behind the idea that electromagnetic radiation can be described either by a wave model or a particle model, and that for some situations one model is more useful than the other. [Clarification Statement: Emphasis is on how the experimental evidence supports the claim and how a theory is generally modified in light of new evidence. Examples of a phenomenon could include resonance, interference, diffraction, and photoelectric effect.] [Assessment Boundary: Assessment does not include using quantum theory.]

HS-PS4-3

Tandem Mass Spectrometry for Biomolecule Analysis

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