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

タンデム質量分析法

タンデム質量分析法における関心の生体分子は生体試料から分離され、その組成とシーケンスを明らかにするために複数のサブユニットに断片化されました。これは、シリーズの質量分析装置を持っていることで。最初の分光計は、特定質量比を充電するためのサンプルとフィルター イオンをイオン化します。フィルター処理されたイオンは断片化し、フラグメントの分析、2 つ目の質量分析計に渡されます。
このビデオは、質量比の選択と解離のメソッドを含むタンデム質量分析法の原則を紹介します。また生化学的化合物を分析するための一般的な手順で使用しているタンデム質量分析法による衝突誘起解離。アプリケーションでは、監視、タンパク質翻訳後修飾の定量およびタクロリムス血中濃度の検出選択反応を説明します。
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タンデム質量分析のリンクが最初に質量分析の複数の段階、生体分子を分離、化学構造の側面を確認して一緒に。生体は、その分子の組成を決定し難い大規模で複雑な構造を持ちます。タンデム質量分析は、後で識別・ シーケンスを明らかに助けることができる複数のサブユニットに断片化している興味の分子を選択します。このビデオでは、生化学のタンデム質量分析法の概念、一般的な手順とその利用方法のいくつかが表示されます。
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典型的な仕様質量計測器としてタンデム質量分析を開始: イオン源、イオン、および質量分析器にサンプルを変換するとイオンの質量電荷比に基づいて分離します。他は装置の棒に衝突しながら、共通の質量分析器、四重極は、特定の割合でイオンをのみ使用できます。認められれば、種前駆イオンと呼ばれる興味の生体分子であります。イオンに衝突セル、通常別の四重極、フラグメントを予測可能なパターンでイオンにエネルギーを適用する場所に移動します。
これらのフラグメントは、飛行時間型のこれら「プロダクト イオンを分けるなど、別の質量分析器に移動します。製品イオン、通常 MS の器械のように、検出器に送られます。未知の蛋白質の場合は、結果として得られるスペクトルには生体の決定的な完全なシーケンスを生成困難多数の重複フラグメントが含まれています。しかし、スペクトルのパターンは、特定の蛋白質に一意です。解析ソフトウェアは、重複フラグメントから未知の蛋白質を解明、知られているペプチド配列のデータベースへのスペクトルを比較します。
サンプルと断片化の所望の程度に応じて複数の断片化方式が可能です。断片化のパターンは、エネルギーを転送する方法、その量と前駆イオンを配布する方法に依存します。エネルギーは、中性粒子や放射線、電子を介して転送することができます。主にそれらの識別に最適なアミノ酸間のペプチド結合の切断中性原子、衝突誘起解離または CID と呼ばれるプロセスを使用しています。
今では技術の基礎をカバーしている、細菌の細胞の封筒のコンポーネントを研究に使用されている CID タンデム質量分析法を見てみましょう。
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すべての質量分析実験と同様、最初の手順は、サンプルをイオン化するためです。生体分子、マトリックス支援レーザー脱離エレクトロ スプレー イオン化とこれは通常です。前駆物質イオン信号は、イオン光学系のチューニングによって、最適化されます。ターゲットが分離されれば、および断片化メソッドを選択すると、CID など。
衝突のセルに前駆イオンを加速する、電圧印加の強さは、断片化の程度を影響します。前駆体がほぼ最高製品イオンと比較して 10% 豊富になるまで、この電圧が増加します。複数スペクトルが取得され、十分な信号対雑音比を達成するまでの平均します。必要スキャン数は元の前駆イオンの信号強度に依存して、3 から 300 までの範囲をすることができます。
この例では、エシェリヒア属大腸菌 K-12 から脂質 A の検体は、CID 後 19 主なフラグメントを持っていた。リピド A の構造はよく知られている、サンプルから特定の構成を再構築するためのソフトウェアを許可します。
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今では手順を見てきた、いくつかの生化学のタンデム質量分析法を使用する方法を見てみましょう。
タンデム質量分析法における一般的なスキャン モードは選択した反応の監視、または SRM です。SRM では、両方の質量分析装置は、前駆体および製品、特定のイオンに焦点を当て、選択した質量電荷比に固定されます。SRM の感度の高いのためペプチド濃度既知の標準スペクトルを利用し、定量化する興味の蛋白質をできるように、未知のサンプルを比較できます。、
タンパク質一般官能基のメチル基、リン酸基、糖鎖と呼ばれる糖などの添加により通常翻訳後変更されます。これらは細胞シグナリング プロセス、細胞が互いに通信する方法の解明に重要です。タンデム質量分析法より小さいコンポーネントに蛋白質をフラグメント化、ため特定のフラグメントまたはアミノ酸も PTM の位置を特定することが可能です。アセチル化とトリメチルなどのいくつかの変更は、クロマト グラフ分離は、質量分析の前に行われるだけで、質量を区別することは困難。
患者の血液で多くの検体は、典型的な質量分析法の検出限界以下の濃度で発見されます。SRM の別の利点は、すべてが 1 つの製品のイオン、感度、検出下限値を最大 100 倍に強化を破棄です。この例では、タクロリムス、免疫抑制薬は、1 ng/mL のレベルで検出できます。
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タンデム質量分析法でゼウスのビデオを見てきただけ。このビデオ計測器の理論を説明した、一般的な手順行き、手法が現在使用されている方法のいくつかを説明しました。見てくれてありがとう!
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In tandem mass spectrometry a biomolecule of interest is isolated from a biological sample, and then fragmented into multiple subunits in order to help ...

タンデム質量分析は、質量分析の複数の段階をリンクして、最初に生体分子を分離し、次にその化学組成の側面を決定します。生体分子は大きく複雑な構造を持っているため、その分子組成を決定することは困難です。タンデム質量分析は、目的の分子を選択し、後で複数のサブユニットに断片化することで、その同定と配列の解明に役立ちます。このビデオでは、タンデム質量分析の概念、一般的な手順、および生化学におけるその使用の一部を示します。タンデム質量分析は、サンプルをイオンに変換するイオン源と、イオンを質量電荷比に基づいて分離する質量分析器を備えた典型的な質量分析装置として始まります。一般的な質量分析器である四重極は、特定の比率のイオンのみを通過させますが、他のイオンは装置のロッドに衝突します。通過を許された分子種は、プリカーサーイオンと呼ばれ、目的の生体分子です。イオンはコリジョンセル(通常は別の四重極)に移動し、そこでエネルギーが印加されて予測可能なパターンでイオンが断片化されます。これらのフラグメントは、Time-of-Flightなどの別の質量分析器に移動し、これらの「プロダクトイオン」を分離します。その後、プロダクトイオンは、通常のMS装置と同様に検出器に送られます。未知のタンパク質の場合、得られるスペクトルには多数の重なり合うフラグメントが含まれているため、生体分子の決定的な完全な配列を生成することが困難になります。ただし、スペクトルパターンは特定のタンパク質に対して一意です。解析ソフトウェアは、スペクトルを既知のペプチド配列のデータベースと比較し、オーバーラップするフラグメントから未知のタンパク質を解明します。サンプルと必要なフラグメンテーションの程度に応じて、複数のフラグメンテーション方法が可能です。フラグメンテーションパターンは、エネルギーの移動方法、その量、およびプリカーサーイオンを介したエネルギーの分布方法によって異なります。エネルギーは、中性粒子、放射線、または電子を介して伝達できます。中性原子を用いることで、衝突誘起解離(CID)と呼ばれるプロセスは、主にアミノ酸間のペプチド結合で切断され、アミノ酸の同定に理想的です。この手法の基本がわかったところで、細菌細胞エンベロープの成分を研究するために使用されているCIDタンデム質量分析を見てみましょう。すべての質量分析実験と同様に、最初のステップはサンプルをイオン化することです。生体分子の場合、これは通常、マトリックス支援レーザー脱離またはエレクトロスプレーイオン化によって行われます。次に、イオン光学系のチューニングにより、プリカーサーイオンシグナルが最適化されます。完了すると、ターゲットが分離され、CIDなどのフラグメンテーション方法が選択されます。プリカーサーイオンをコリジョンセルに加速する印加電圧の強度は、フラグメンテーションの程度に影響します。この電圧は、前駆体が最高生成物イオンと比較して約10%の存在量になるまで増加します。複数のスペクトルが取得され、十分なS/N比が達成されるまで平均化されます。必要なスキャン回数は、元のプリカーサーイオンのシグナル強度に依存し、3〜300の範囲です。この例の分析種は、大腸菌K-12由来の脂質Aで、CID後に19の主要なフラグメントがありました。脂質Aの一般的な構造はよく知られているため、ソフトウェアはサンプルから特定の組成を再構築できます。手順を見てきたところで、生化学におけるタンデム質量分析の使用方法をいくつか見てみましょう。タンデム質量分析の一般的なスキャンモードは、選択反応モニタリング(SRM)です。SRMでは、両方の質量分析計が選択した質量電荷比に固定され、特定のプリカーサーイオンと製品イオンに焦点を当てています。SRMは感度が高いため、既知の濃度のペプチドスタンダードのスペクトルを利用して、未知のサンプルのスペクトルと比較することで、目的のタンパク質を定量することができます。タンパク質は、通常、メチル基、リン酸基、糖などの官能基(グリカン)の付加によって、翻訳後に修飾されます。これらは細胞シグナル伝達プロセスにおいて重要であり、細胞が互いにどのように通信するかを解明します。タンデム質量分析はタンパク質をより小さな成分に断片化するため、PTMが特定のフラグメントやアミノ酸に位置を特定することができます。アセチル化やトリメチル化などの一部の修飾は、質量だけでは区別が難しいため、質量分析の前にクロマトグラフィー分離を行います。患者の血液中の多くの分析種は、一般的な質量分析の検出限界を下回る濃度で検出されます。SRMのもう一つの利点は、1つの製品イオンを除くすべての製品イオンを破棄し、感度を向上させ、検出下限を最大100倍に向上させることです。この例では、免疫抑制剤であるタクロリムスを 1 ng/mL のレベルで検出できます。JoVEのタンデム質量分析に関するビデオをご覧になりました。このビデオでは、機器の理論を説明し、一般的な手順を説明し、現在この技術がどのように利用されているかを説明しました。ご覧いただきありがとうございます!

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Biochemistry

生化学

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

このコレクションでは、親和性クロマトグラフィーなどの一般的に使用される精製方法や、MALDI-TOFなどの分析方法について紹介します。さらに、共同免疫沈降法や代謝標識法など、生体分子の相互作用や機能を評価する方法も紹介します。

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 ...

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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 ...

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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 ...

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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 ...

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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 ...

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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.]

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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, ...

reconstruction-of-signal-using-interpolation

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.]

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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

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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