Name: how amino acid sequence shapes proteins
Uploaded: 2023-04-30T10:34:15.000Z
Duration: 1 min 25 s
Channel: JoVE

K12 Standards

Next Generation Science Standards

High School

Life Science

from-molecules-to-organisms-structures-and-processes

From Molecules to Organisms: Structures and Processes

HS-LS1-1

Protein Folding

In einem neu synthetisierten Peptid leiten Wechselwirkungen zwischen seinen konstituierenden Aminosäuren seine Faltung zu einer stabilen dreidimensionalen Struktur, die als native Konformation bezeichnet wird, oft in seiner funktionellen Form.
Zunächst faltet sich die lineare Polypeptidkette durch Wasserstoffbrückenbindungen zwischen Aminosäureresten in Alpha-Helices und Beta-Faltblätter.
Hydrophobe Seitenketten, die aus den Helices oder Beta-Faltblättern herausragen, kommen zusammen und entfernen umliegende Wassermoleküle. Infolgedessen wird das Polypeptid in ein locker gefaltetes Zwischenprodukt mit einem hydrophoben Kern gepackt.
Polare Reste auf der Oberfläche bilden zusätzliche Wasserstoffbrückenbindungen und ionische Wechselwirkungen, während benachbarte Cysteine kovalente Disulfidbindungen bilden, um das Protein in seiner nativen Konformation zu stabilisieren.
Bei Proteinen mit mehreren Cysteinen katalysiert das Proteindisulfid-Isomerase-Enzym den schnellen Austausch von Thiolgruppen und ermöglicht so eine korrekte Bildung von Disulfidbindungen.
Die meisten Proteine falten sich nicht von selbst und werden durch Hitzeschockproteine und Chaperonine unterstützt.
Diese molekularen Chaperone beschleunigen den Faltungsprozess, indem sie das entfaltete Peptid binden und die Aggregation verhindern oder eine Mikroumgebung schaffen, in der sich das Peptid in seine native Konformation falten kann.

<ol>
	<li>Lodish, Harvey et al. Molekulare Zellbiologie. 8. Aufl. W.H. Freeman und Company, 2016. Seiten 81-85</li>
	<li>Donald Voet und Judith G Voet Biochemie. 4. Aufl. JOHN WILEY & SONS, INC. 2011. Seiten 278-290</li>
	<li>Nelson und Cox, Lehninger, Prinzipien der Biochemie, 7. Aufl. W.H. Freeman and Company, 2016. Seiten 396-407</li>
</ol>

proteinfaltung

Proteine sind Ketten von Aminosäuren, die durch Peptidbindungen miteinander verbunden sind. Bei der Synthese faltet sich ein Protein in eine dreidimensionale Konformation, die für seine biologische Funktion entscheidend ist. Wechselwirkungen zwischen seinen Aminosäurebestandteilen steuern die Proteinfaltung, und daher hängt die Proteinstruktur in erster Linie von seiner Aminosäuresequenz ab.

Die Proteinstruktur ist entscheidend für ihre biologische Funktion

Proteine erfüllen ein breites Spektrum an biologischen Funktionen, wie z. B. die Katalyse chemischer Reaktionen, die Bereitstellung von immunologischer Abwehr, Speicherung, Transport, zellulärer Kommunikation, Bewegung und struktureller Unterstützung. Die Funktion eines Proteins hängt hauptsächlich davon ab, andere Moleküle zu erkennen und zu binden, analog zu einem Schloss und einem Schlüssel. Daher hängt die spezifische Aktivität jedes Proteins von seiner einzigartigen dreidimensionalen Architektur ab.

Damit ein Protein funktionsfähig ist, muss es sich genau falten. Die meisten Proteine durchlaufen mehrere Zwischenformen, bevor sie sich in die stabilste, biologisch aktive Struktur falten. Eine Fehlfaltung von Proteinen kann die Gesamtfunktion der Zelle beeinträchtigen. Die Anhäufung fehlgefalteter oder entfalteter Proteine beim Menschen führt zu Mukoviszidose, Alzheimer, Parkinson, amyotropher Lateralsklerose und der Creutzfeldt-Jakob-Krankheit.

Kritische Determinanten der Proteinstruktur

Proteine bestehen aus einer oder mehreren Ketten von Aminosäuren, den sogenannten Polypeptiden. Ein Polypeptid wird als lineare Kette synthetisiert, die sich schnell in sich selbst faltet und eine dreidimensionale Struktur bildet. Die Begriffe Polypeptid und Protein werden manchmal synonym verwendet, am häufigsten wird jedoch ein gefaltetes Polypeptid, das eine biologische Funktion erfüllen kann, als Protein bezeichnet. Eine Proteinstruktur wird normalerweise auf vier Ebenen beschrieben: primär, sekundär, tertiär und quartär. Die meisten Polypeptide falten sich zu einer insgesamt kompakten, kugelförmigen Tertiärstruktur zusammen, wie zum Beispiel Hämoglobin, das Sauerstoff transportierende Protein im Blut. Einige Proteine wie Keratine bilden lange Fasern und kommen häufig in Haaren und Nägeln vor. Im Gegensatz zu faserförmigen Proteinen sind globuläre Proteine wasserlöslich.

Die Reihenfolge der Aminosäuren in der Polypeptidkette ist der wichtigste Faktor für deren Struktur. Die Aminosäuresequenz bestimmt die Art und Lage der Sekundärstrukturen. Darüber hinaus wird die gesamte Tertiärstruktur eines Proteins überwiegend durch chemische Bindungen zwischen Aminosäureseitenketten stabilisiert – den einzigartigen chemischen Gruppen, die Aminosäuren voneinander unterscheiden. Diese Seitenketten sind entweder geladen (positiv oder negativ), polar-ungeladen oder unpolar.

Abhängig von ihren Seitenkettengruppen weisen die Aminosäuren einzigartige physikalische und chemische Eigenschaften auf. Polare und geladene Aminosäuren interagieren beispielsweise mit Wasser unter Bildung von Wasserstoffbrückenbindungen und werden als hydrophil bezeichnet. Im Gegensatz dazu vermeiden die unpolaren Aminosäuren Wechselwirkungen mit Wasser und werden als hydrophob bezeichnet. Wenn ein Protein in einer zellulären Umgebung gefaltet wird, werden daher Seitenketten hydrophober Aminosäuren im Kern des Proteins vergraben, entfernt von der wässrigen Umgebung. Im Gegensatz dazu liegen die hydrophilen Aminosäureseitenketten auf der Oberfläche des Proteins frei.

Die dicht gepackten hydrophoben Aminosäuren im Proteinkern führen zur Bildung schwacher Van-der-Waals-Wechselwirkungen zwischen den Seitenkettengruppen. Diese Van-der-Waals-Kräfte verleihen dem gefalteten Protein zusätzliche Stabilität. Die auf der Proteinoberfläche freigelegten polaren Aminosäuren können Wasserstoffbrückenbindungen mit Wassermolekülen oder anderen polaren Aminosäureseitenketten bilden. Die positiv und negativ geladenen Aminosäuren befinden sich auch auf der Außenseite eines Proteins, wo sie Ionenbindungen mit anderen benachbarten, entgegengesetzt geladenen Aminosäuren eingehen.

Disulfidbindungen bilden sich zwischen zwei Sulfhydryl- oder SH-Gruppen an der Aminosäure Cystein. Dabei handelt es sich um eine robuste Wechselwirkung, die wie eine Verstärkung auf das gefaltete Protein wirkt. Disulfidbrücken fixieren das gefaltete Protein in seiner bevorzugten dreidimensionalen Konformation. Die ordnungsgemäße Faltung eines Proteins hängt auch von anderen Faktoren der Zellumgebung wie pH-Wert, Salzkonzentration, Temperatur usw. ab. Änderungen der physikalischen und chemischen Bedingungen in einer Proteinumgebung wirken sich auf die chemischen Wechselwirkungen aus, die das Protein zusammenhalten, und können zu einer Fehlfaltung des Proteins führen oder sich entfalten und seine biologische Funktion verlieren – ein Prozess, der als Proteindenaturierung bekannt ist.

Proteinfaltung

Proteine sind Ketten von Aminosäuren, die durch Peptidbindungen miteinander verbunden sind. Bei der Synthese faltet sich ein Protein zu einer dreidimensionalen Konformation, die für die ...

Education

Lehre

JoVE Core

Cell Biology

Zellbiologie

Unit 1

Einheit 1

Protein Structure

Proteinstruktur

KEY TERMS AND CONCEPTS

KERNBEGRIFFE UND KONZEPTE

how amino acid sequence shapes proteins

Proteins get their shape from the order of amino acids in a polypeptide chain. After a protein is made, the chain folds into a three-dimensional form that is needed for it to work. The way amino acids interact with one another guides this folding.

Protein structure matters because proteins do many jobs in cells. They can speed up chemical reactions, help with immune defense, store materials, carry substances, send cell signals, support movement, and provide structure. A protein usually works by binding to another molecule, much like a lock and key. That is why its specific three-dimensional shape is so important.

To be functional, a protein must fold correctly. Many proteins pass through several intermediate forms before reaching the most stable and biologically active shape. When proteins misfold, they can disrupt cell function. In humans, misfolded or unfolded proteins are linked with cystic fibrosis, Alzheimer’s disease, Parkinson’s disease, amyotrophic lateral sclerosis, and Creutzfeldt-Jakob disease.

Proteins are made of one or more amino acid chains called polypeptides. A polypeptide starts as a linear chain and then folds quickly into a three-dimensional structure. The words polypeptide and protein are sometimes used interchangeably, but a folded polypeptide that can do a job is usually called a protein. Protein structure is often described at four levels: primary, secondary, tertiary, and quaternary.

Most polypeptides fold into a compact, globular tertiary structure. Hemoglobin, the oxygen-carrying protein in blood, is an example. Some proteins, such as keratins, form long fibers and are found in hair and nails. Globular proteins are usually soluble in water, while fibrous proteins are not.

The amino acid sequence is the main factor that determines protein shape. It helps decide where secondary structures form and how the full tertiary structure develops. Side chains, the chemical groups that make amino acids different from one another, stabilize the folded protein. These side chains may be charged, polar but uncharged, or non-polar.

Polar and charged amino acids interact with water and are called hydrophilic. Non-polar amino acids avoid water and are called hydrophobic. When a protein folds in a cell, hydrophobic side chains are usually buried in the core, away from water, while hydrophilic side chains stay on the surface. Tight packing in the hydrophobic core creates weak Van der Waals interactions that help stabilize the structure.

Hydrophilic side chains on the outside can form hydrogen bonds with water or with other polar side chains. Positively and negatively charged amino acids can also form ionic bonds with nearby oppositely charged amino acids. Another strong bond, called a disulfide bond, forms between two sulfhydryl, or SH, groups on cysteine. This bond helps lock the protein into its most stable three-dimensional shape.

Protein folding also depends on the cell’s environment. pH, salt concentration, and temperature can affect the chemical interactions that hold a protein together. If these conditions change, a protein may misfold or unfold and lose its function. This process is called protein denaturation.

How Amino Acid Sequence Shapes Proteins

what are proteins?

Protein Building Blocks and Folding

Proteins are built from amino acids linked by peptide bonds. Long chains of amino acids are often called polypeptides, and the terms proteins and polypeptides are sometimes used the same way. In this context, polypeptides with a molecular weight below 10,000 daltons are called polypeptides, while proteins have a higher molecular weight. Very short chains with fewer than 20 amino acids are called peptides or oligopeptides. Amino acids are the basic units of proteins. Each amino acid has a...

protein organization

Protein Folding Levels and Bonds

Proteins are built from amino acids and folded into shapes that support many cell jobs. They help with DNA replication, molecular transport, catalysis, and structural support. Their function depends on how their amino acids are arranged and folded. Protein structure is organized in levels. The primary structure is the amino acid sequence in a polypeptide chain. Amino acids are joined by peptide bonds, and the chain has two ends: the amino terminus, or N-terminus, and the carboxyl terminus, or...

protein folding

Proteins get their shape from the order of amino acids in a polypeptide chain. After a protein is made, the chain folds into a three-dimensional form that is needed for it to work. The way amino acids interact with one another guides this folding. Protein structure matters because proteins do many jobs in cells. They can speed up chemical reactions, help with immune defense, store materials, carry substances, send cell signals, support movement, and provide structure. A protein usually works...

protein families

Protein Families and Superfamilies

Protein families and superfamilies group proteins with shared features. These groups help scientists organize proteins by common structure, function, or evolutionary history. The classification can show how related proteins are connected across different organisms. A protein family usually includes proteins that are closely related. A superfamily is a broader group that can include several families with more distant relationships. These categories help explain why some proteins share similar...

conservation of protein domains

Protein Domains Shared Across Proteins

Protein domains are shared structural and functional parts of proteins. A domain is a region that can often be found in more than one protein, even when the full proteins are different. This conservation means that a protein domain may keep a similar shape or role across related proteins. Because of that, scientists can compare proteins by looking for domains that stay the same. Conserved domains help reveal how proteins are related and how they may work. The topic of protein domain...

globular and fibrous proteins

Protein Shapes: Globular vs Fibrous

Proteins can have globular or fibrous shapes, and these shapes help explain how they work in the body. Globular proteins are compact and usually fold into rounded forms. Fibrous proteins are long, extended molecules that often provide support and structure. The shape of a protein is tied to its function. Globular proteins often take part in chemical jobs in cells, while fibrous proteins are better suited for strength and stability. These structural differences make the two groups easy to...

intrinsically disordered proteins

Flexible Protein Regions and Disorder

Intrinsically disordered proteins have flexible regions that do not settle into one fixed shape. Instead, these proteins can remain dynamic and change form as they move through the cell. This flexibility is an important part of their structure and function. Many proteins need a stable folded shape to work properly. Intrinsically disordered proteins are different because they may lack a single rigid structure under normal conditions. Their shifting shape can help them take part in cell...

protein complex assembly

Protein Complex Formation and Function

Protein complex formation explains how proteins join together to carry out specific jobs in cells. These groups are called protein complexes, and they can form in more than one way. Some complexes are homomeric, which means they contain the same kind of protein subunit. Others are heteromeric, which means they contain different protein subunits. The assembly process helps show how protein shape and subunit choice affect function. When proteins combine, the resulting complex can behave...

conjugated proteins

Conjugated Proteins and Their Bound Groups

Conjugated proteins are proteins that include a nonprotein part called a prosthetic group. This added group helps give the protein its full structure or function. The video explains how the protein part and the bound group work together. Several common types of conjugated proteins are named by the kind of group attached. Nucleoproteins contain nucleic acids. Glycoproteins contain carbohydrate groups, and lipoproteins contain lipid groups. Other examples include phosphoproteins, which have...

amyloid fibrils

Amyloid Fibrils and Protein Aggregation

Amyloid fibrils are protein aggregates with a very specific structure. They are made when proteins misfold and stick together in long, ordered fibers. This structure makes them different from many other protein clumps. Amyloid fibrils are important in biology because they are linked to protein aggregation. Protein aggregation means proteins build up into groups instead of staying properly folded and separate. In many cases, this process is associated with disease and abnormal cell function. <br...

key terms and concepts

Learn how amino acid sequence, side-chain interactions, and cell conditions shape protein structure, stability, and function in high school biology.

How Amino Acid Sequence Shapes Proteins | JoVE K12

cell biology

JoVE Core Zellbiologie veranschaulicht komplexe zelluläre Prozesse in leicht verständlichen und dennoch umfassenden animierten Videolektionen. Diese Sammlung konzentriert sich auf die wesentlichen Bestandteile und Funktionen von Zellen, einschließlich Organellen und Membranen, Zelltransport und Zellenergie. Ergänzt wird sie durch Videos von Wissenschaftlern in Aktion, die die Anwendung der Zellbiologie in realen Forschungsexperimenten demonstrieren.

new-york-state-science-learning-standards

New York State Science Learning Standards

Structure and Function

HS-LS1-1.

Characteristics of Life

Biology is a natural science that studies life and living organisms, including their structure, function, development, interactions, evolution, ...

https://cloudfront.jove.com/files/media/science-education/science-education-thumbs/10647.jpg

Cell Structure

Background
Cells represent the most basic biological units of all organisms, whether it be simple, single-celled organisms like bacteria, or large, ...

Visualizing Onion and Cheek Cells
ExpandImmediately before the experiment, wash and peel onion bulbs for the class.
Remove the entire brown outer skin and ...

Visualizing Onion and Human Cells
ExpandIn this experiment you will prepare different types of cells from a plant and animal, onion and human ...

What are Cells?

Cell Diversity

The concept of a cell started with microscopic observations of dead cork tissue by Robert Hooke in 1665. Hooke coined the term &#34;cell&#34; based on the ...

Cytoplasm

The cytoplasm consists of organelles and a framework of protein scaffolds called the cytoskeleton suspended in an aqueous solution, the cytosol. The ...

The Nucleus

The nucleus is a membrane-bound organelle that acts as a control center in a eukaryotic cell. It contains chromosomal DNA, which controls gene expression ...

The Central Dogma

The DNA Helix

Nucleic Acids

DNA as a Genetic Template

Structure of a Gene

A gene is the fundamental unit of heredity. Every individual has two copies of each gene, one inherited from each parent. Although most people contain the ...

Chromosome Structure

Base-pairing and DNA Repair

What is Gene Expression?

A gene is a stretch of DNA that serves as the blueprint for functional RNAs and proteins. Since DNA is comprised&#160; of nucleotides and proteins are ...

RNA Structure

The basic structure of RNA consists of a string of ribonucleotides attached by phosphodiester bonds. Although most RNA is single-stranded, it can form ...

Protein Families

Types of RNA

Three main types of RNA are involved in protein synthesis: messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA). These RNAs perform diverse ...

Conservation of Protein Domains

Transcription

Transcription is the synthesis of RNA from a DNA sequence by RNA polymerase. It is the first step in producing a protein from a gene sequence. ...

Globular and Fibrous Proteins

Translation

Translation is the process of synthesizing proteins from the genetic information carried by messenger RNA (mRNA). Following transcription, it constitutes ...

Intrinsically Disordered Proteins

Ribosomes

Ribosomes translate genetic information encoded by messenger RNA (mRNA) into proteins. Both prokaryotic and eukaryotic cells have ribosomes. Cells that ...

Protein Complex Assembly

Protein and Protein Structures

Conjugated Proteins

Proteins: From Genes to Degradation

Amyloid Fibrils

What are Proteins?

Proteins are polymers of amino acids linked together by peptide bonds. Proteins and polypeptides are interchangeably used to refer to long chains of amino ...

Ligand Binding Sites

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular ...

Protein-Protein Interfaces

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to ...

Conserved Binding Sites

Cofactors and Coenzymes

Enzymes are proteins made of amino acids. The functional group of each constituent amino acid catalyzes a wide variety of chemical reactions via ionic ...

Cooperative Allosteric Transitions

Protein Kinases and Phosphatases

GTPases and their Regulation

Covalently Linked Protein Regulators

protein-complexes-with-interchangeable-parts

Protein Complexes with Interchangeable Parts

Mechanical Protein Function

Structural Protein Function

Protein Networks

Construct an explanation based on evidence for how the structure of DNA determines the structure of proteins, which carry out the essential functions of life through systems of specialized cells. [Assessment Boundary: Assessment does not include identification of specific cell or tissue types, whole body systems, specific protein structures and functions, or the biochemistry of protein synthesis.]

Levels of Organization

Biological organization is the classification of biological structures, ranging from atoms at the bottom of the hierarchy to the Earth&#x27;s biosphere. ...

Animal and Plant Cell Structure

Animal and plant cells not only differ in their structure, function, and mode of nutrition but also in how they reproduce, specialize, and organize into ...

structural-organization-of-the-human-body-an-overview

Structural Organization of the Human Body: An Overview

It is convenient to consider the body&#39;s structures in terms of fundamental levels of organization that increase in complexity: subatomic particles, ...

Overview of Human Digestion

The human body contains a monogastric digestive system. In a monogastric digestive system, the stomach only contains one chamber in which it digests food. ...

Anatomy of the Intestines

Although digestion of proteins, carbohydrates, and lipids may begin in the stomach, it is completed in the intestine. The absorption of nutrients, water, ...

Accessory Organs

Accessory organs are those that participate in the digestion of food but do not come into direct contact with it like the mouth, stomach, or intestine do. ...

Lipid Digestion

Lipids are large molecules that are generally not water-soluble. Since most of the digestive enzymes in the human body are water-based, there are specific ...

Protein Digestion

Protein digestion begins in the stomach, where the highly acidic environment can easily disrupt protein structure by exposing the peptide bonds of ...

Carbohydrate Digestion

Carbohydrate digestion and metabolism break down simple and complex carbohydrates from food into saccharides (i.e., sugars) for the body to use as energy. ...

What is a Nervous System?

Overview

The nervous system is the collection of specialized cells responsible for maintaining an organism&rsquo;s internal environment and coordinating ...

The Parasympathetic Nervous System

Overview

The parasympathetic nervous system is one of the two major divisions of the autonomic nervous system. This parasympathetic system is responsible ...

The Sympathetic Nervous System

Overview

The sympathetic nervous system&mdash;one of the two major divisions of the autonomic nervous system&mdash;is activated in times of stress. It ...

Oogenesis

In human women, oogenesis produces one mature egg cell or ovum for every precursor cell that enters meiosis. This process differs in two unique ways from ...

What is a Sensory System?

Sensory systems detect stimuli&mdash;such as light and sound waves&mdash;and transduce them into neural signals that can be interpreted by the nervous ...

Fertilization

During fertilization, an egg and sperm cell fuse to create a new diploid structure. In humans, the process occurs once the egg has been released from the ...

What is the Skeletal System?

Overview

The adult human skeleton comprises 206 bones that are connected through cartilage, tendons, and ligaments. The skeleton provides a rigid ...

an-introduction-to-the-zebrafish-danio-rerio

An Introduction to the Zebrafish: Danio rerio

Zebrafish (Danio rerio) are small freshwater fish that are used as model organisms for biomedical research. The many strengths of these fish include their ...

Physiology of the Circulatory System

Homeostasis
Conditions in the external environment of an organism can change rapidly and drastically. To survive, organisms must maintain a fairly ...

Anatomy of the Circulatory System

The human circulatory system consists of blood, blood vessels that carry blood away from the heart, around the body, and back to the heart, and the heart ...

Measuring Blood Pressure
ExpandTo prepare for the blood pressure exercise, simply place the appropriate number of alcohol swabs, sphygmomanometers, and ...

Anatomy of the Heart

The human heart is made up of three layers of tissue that are surrounded by the pericardium, a membrane that protects and confines the heart. The ...

Measuring Circulatory System Function in Humans
ExpandBefore starting the experiment go to the front of the room and collect an alcohol swab, a ...

Blood Flow

Blood is pumped by the heart into the aorta, the largest artery in the body, and then into increasingly smaller arteries, arterioles, and capillaries. The ...

What Are Osmoregulation and Excretion?

Organisms must keep bodily fluids at a constant temperature and pH while maintaining specific solute concentrations in order to support life functions. ...

Blood Withdrawal I

Source: Kay Stewart, RVT, RLATG, CMAR; Valerie A. Schroeder, RVT, RLATG. University of Notre Dame, IN
Blood collection is a common requirement for ...

Kidney Structure

The kidneys are two large bean-shaped organs located in the upper abdomen. They filter the blood several times a day to remove toxins and rebalance water ...

Blood Withdrawal II

Source: Kay Stewart, RVT, RLATG, CMAR; Valerie A. Schroeder, RVT, RLATG. University of Notre Dame, IN
The collection of blood from mice and rats for ...

What is the Immune System?

Overview

The immune system comprises diverse biological structures and processes that protect the body from disease. These processes can be classified ...

Bone Remodeling

Bone remodeling is a continuous and balanced process of bone resorption by osteoclasts and bone formation by osteoblasts. In adults, it helps maintain ...

Spermatogenesis

Spermatogenesis is the process by which haploid sperm cells are produced in the male testes. It starts with stem cells located close to the outer rim of ...

Bone Structure

Within the skeletal system, the structure of a bone, or osseous tissue, can be exemplified in a long bone, like the femur, where there are two types of ...

Breathing

The process of breathing, inhaling and exhaling, involves the coordinated movement of the chest wall, the lungs, and the muscles that move them. Two ...

Develop and use a model to illustrate the hierarchical organization of interacting systems that provide specific functions within multicellular organisms. [Clarification Statement: Emphasis is on functions at the organism system level such as nutrient uptake, water delivery, and organism movement in response to neural stimuli. An example of an interacting system could be an artery depending on the proper function of elastic tissue and smooth muscle to regulate and deliver the proper amount of blood within the circulatory system.] [Assessment Boundary: Assessment does not include interactions and functions at the molecular or chemical reaction level.]

HS-LS1-2

What is Homeostasis?

Maintaining homeostasis requires that the body continuously maintain its internal conditions. Each physiological condition has a particular set point, ...

Negative and Positive Feedback

Homeostatic Imbalance

Homeostasis is the maintenance of a stable internal environment within the body, which is crucial for the proper functioning of cells, tissues, organs, ...

pH Homeostasis

Acid-base homeostasis is essential for maintaining normal physiological activities in humans. The pH of various body fluids is strictly regulated because ...

Plan and conduct an investigation to provide evidence that feedback mechanisms maintain homeostasis. [Clarification Statement: Examples of investigations could include heart rate response to exercise, stomate response to moisture and temperature, and root development in response to water levels.] [Assessment Boundary: Assessment does not include the cellular processes involved in the feedback mechanism.]

HS-LS1-3

How Amino Acid Sequence Shapes Proteins

Description

Transcript

Tags

More videos by Standards