Name: how protein shape determines function
Uploaded: 2023-04-30T18:28:47.000Z
Duration: 2 min 15 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 and Protein Structures

Proteine sind Polymere aus Aminosäuren, die durch Peptidbindungen miteinander verbunden sind. Die meisten Proteine falten sich zu spezifischen dreidimensionalen Strukturen, um ihre Funktion zu erfüllen.
Die Proteinstruktur wird in vier Kategorien eingeteilt: primär, sekundär, tertiär und quartär.
Die lineare Abfolge der Aminosäuren im Protein ist seine Primärstruktur. Diese Sequenzen werden in der Reihenfolge der Polymersynthese abgelesen, vom N-Terminus, dem freien Aminoende, bis zum C-Terminus, dem freien Carboxylende.
Sekundärstrukturen bilden sich durch Wasserstoffbrückenbindungen zwischen dem Sauerstoff aus der Carbonylgruppe einer Aminosäure und dem Wasserstoff aus der Aminogruppe einer anderen. Zu den gängigen Sekundärstrukturen gehören α-Helices und β-Plissee-Platten. 
Diese und andere Verbindungsstrukturen, wie z. B. β-Windungen, interagieren weiter und bilden die dreidimensionale Struktur des Proteins, die als Tertiärstruktur bezeichnet wird.
Die Bildung der Tertiärstruktur erfolgt durch Wechselwirkungen zwischen den R-Gruppen der Aminosäuren.
R-Gruppen mit entgegengesetzten Ladungen können ionische Bindungen bilden, und Schwefel in zwei Cysteinen kann eine kovalente Disulfidbrücke bilden. Weitere Faktoren sind hydrophobe Wechselwirkungen zwischen hydrophoben Seitenketten und Wasserstoffbrückenbindungen zwischen polaren Seitenketten.
Darüber hinaus bilden einige Proteine quartäre Strukturen, Anordnungen von zwei oder mehr Polypeptidketten. Zum Beispiel ist Hämoglobin ein Protein, das aus vier Untereinheiten besteht, zwei α und zwei β.
Wissenschaftler können die Struktur eines Proteins nutzen, um seine Funktion und Position in einer Zelle vorherzusagen. Proteine im Zellzytoplasma haben hydrophile Aminosäuren auf ihren Oberflächen, die mit dem Wasser im Zytoplasma interagieren und hydrophobe Kerne haben.
Im Gegensatz dazu haben Proteine, die in Zellmembranen vorhanden sind, oft hydrophobe Aminosäuren auf der Oberfläche, die mit Glycerophospholipiden in der Membran interagieren und hydrophile Kerne haben.

<ol>
	<li>Nelson, D. L., & Cox, M. M. (2008). Lehninger Prinzipien der Biochemie (5. Aufl.). W.H. Freeman. Seite 113-140</li>
	<li>Kristallstruktur von Hämoglobin im T-Zustand mit Sauerstoffbindung an allen vier Häms.Paoli, M., Liddington, R., Tame, J., Wilkinson, A., Dodson, G. (1996) J Mol Biol 256: 775</li>
</ol>

protein und proteinstrukturen

Proteine ​​sind eines der am häufigsten vorkommenden organischen Moleküle in lebenden Systemen und haben von allen Makromolekülen die vielfältigsten Funktionen. Proteine ​​können strukturelle, regulierende, kontraktile oder schützende Funktionen haben. Sie können beim Transport, bei der Speicherung oder in Membranen eingesetzt werden, oder sie können Toxine oder Enzyme sein. Ihre Strukturen sind ebenso wie ihre Funktionen sehr unterschiedlich. Sie sind jedoch alle Aminosäurepolymere, die in einer linearen Sequenz angeordnet sind. Die Form eines Proteins ist entscheidend für seine Funktion. Beispielsweise kann ein Enzym an seinem aktiven Zentrum ein bestimmtes Substrat binden. Wenn dieses aktive Zentrum aufgrund lokaler Veränderungen oder Änderungen in der gesamten Proteinstruktur verändert wird, ist das Enzym möglicherweise nicht in der Lage, an das Substrat zu binden. Um zu verstehen, wie das Protein seine endgültige Form oder Konformation erhält, müssen wir die vier Ebenen der Proteinstruktur verstehen: primär, sekundär, tertiär und quartär. Primärstruktur Die einzigartige Sequenz von Aminosäuren in einer Polypeptidkette ist ihre Primärstruktur. Das Pankreashormon Insulin beispielsweise hat zwei Polypeptidketten, A und B, die durch Disulfidbrücken miteinander verbunden sind. Die N-terminale Aminosäure der A-Kette ist Glycin, während die C-terminale Aminosäure Asparagin ist.  Die Aminosäuresequenzen in den A- und B-Ketten sind für Insulin einzigartig. Das für das Protein kodierende Gen bestimmt letztendlich die einzigartige Sequenz für jedes Protein. Eine Änderung der Nukleotidsequenz der kodierenden Region des Gens kann dazu führen, dass der wachsenden Polypeptidkette eine andere Aminosäure hinzugefügt wird, was zu einer Änderung der Proteinstruktur und -funktion führt. Bei der Sichelzellenanämie weist die Hämoglobin-β-Kette eine einzelne Aminosäuresubstitution auf, was zu einer Veränderung der Proteinstruktur und -funktion führt. Insbesondere ersetzt Valin in der β-Kette die Aminosäure Glutaminsäure. Aufgrund dieser Veränderung einer Aminosäure in der Kette bilden Hämoglobinmoleküle lange Fasern, die die bikonkaven oder scheibenförmigen roten Blutkörperchen verzerren und dazu führen, dass sie eine Halbmond- oder „Sichelform“ annehmen, was die Blutgefäße verstopft. Dies kann bei den von dieser Krankheit Betroffenen zu unzähligen schwerwiegenden Gesundheitsproblemen wie Atemnot, Schwindel, Kopfschmerzen und Bauchschmerzen führen. Sekundärstruktur Die lokale Faltung des Polypeptids in einigen Regionen führt zur Sekundärstruktur des Proteins. Am häufigsten sind die α-Helix- und β-Faltblattstrukturen. Beide Strukturen werden durch Wasserstoffbrücken in Form gehalten. Die Wasserstoffbrücken bilden sich zwischen dem Sauerstoffatom in der Carbonylgruppe einer Aminosäure und einer anderen Aminosäure, die vier Aminosäuren weiter entlang der Kette liegt. Jede Helixwindung in einer Alpha-Helix hat 3,6 Aminosäurereste. Die R-Gruppen des Polypeptids (die Variantengruppen) ragen aus der α-Helix-Kette heraus. Im β-Faltenblatt bilden Wasserstoffbrückenbindungen zwischen Atomen am Rückgrat der Polypeptidkette die „Falten“. Die R-Gruppen sind an die Kohlenstoffe gebunden und erstrecken sich über und unter den Falten der Falte. Die gefalteten Segmente richten sich parallel oder antiparallel zueinander aus und es bilden sich Wasserstoffbrücken zwischen dem teilweise positiven Wasserstoffatom in der Aminogruppe und dem teilweise negativen Sauerstoffatom in der Carbonylgruppe des Peptidrückgrats. Die α-Helix- und β-Faltblattstrukturen kommen in den meisten globulären und faserigen Proteinen vor und spielen eine wichtige strukturelle Rolle. Tertiärstruktur Die einzigartige dreidimensionale Struktur des Polypeptids ist seine Tertiärstruktur. Diese Struktur ist teilweise auf chemische Wechselwirkungen zurückzuführen, die an der Polypeptidkette wirken. In erster Linie erzeugen die Wechselwirkungen zwischen R-Gruppen die komplexe dreidimensionale Tertiärstruktur des Proteins. Die Art der R-Gruppen in den beteiligten Aminosäuren kann der Bildung der Wasserstoffbrücken entgegenwirken, die wir für Standard-Sekundärstrukturen beschrieben haben. Beispielsweise stoßen sich R-Gruppen mit gleichen Ladungen gegenseitig ab, und solche mit ungleichen Ladungen werden voneinander angezogen (ionische Bindungen). Bei der Proteinfaltung liegen die hydrophoben R-Gruppen der unpolaren Aminosäuren im Inneren des Proteins; wohingegen die hydrophilen R-Gruppen außen liegen. Wechselwirkungen zwischen Cysteinseitenketten bilden in Gegenwart von Sauerstoff Disulfidbindungen, die einzige kovalente Bindung, die während der Proteinfaltung entsteht. Alle diese Wechselwirkungen, ob schwach oder stark, bestimmen die endgültige dreidimensionale Form des Proteins. Wenn ein Protein seine dreidimensionale Form verliert, ist es möglicherweise nicht mehr funktionsfähig. Quartärstruktur In der Natur entstehen einige Proteine aus mehreren Polypeptiden oder Untereinheiten, und das Zusammenspiel dieser Untereinheiten bildet die Quartärstruktur. Schwache Wechselwirkungen zwischen den Untereinheiten tragen zur Stabilisierung der Gesamtstruktur bei. Beispielsweise verfügt Insulin (ein kugelförmiges Protein) über eine Kombination aus Wasserstoff- und Disulfidbindungen, die dazu führen, dass es größtenteils in Kugelform verklumpt. Insulin beginnt als einzelnes Polypeptid und verliert bei posttranslationaler Modifikation einige interne Sequenzen, nachdem die Disulfidbindungen gebildet wurden, die die verbleibenden Ketten zusammenhalten. Seide (ein faseriges Protein) hat jedoch eine β-faltige Blattstruktur, des ist das Ergebnis von Wasserstoffbrückenbindungen zwischen verschiedenen Ketten. Dieser Text wurde angepasst von <a href="https://openstax.org/books/biology-2e/pages/3-4-proteins">Openstax, Biology 2e, Chapter 3.4: Proteins</a>.

Protein und Proteinstrukturen

Proteine gehören zu den am häufigsten vorkommenden organischen Molekülen in lebenden Systemen und haben von allen Makromolekülen den vielfältigsten Funktionsbereich. Proteine können ...

Education

Lehre

JoVE Core

Cell Biology

Zellbiologie

Unit 1

Einheit 1

Biochemistry of the Cell

Biochemie der Zelle

KEY TERMS AND CONCEPTS

KERNBEGRIFFE UND KONZEPTE

how protein shape determines function

Proteins are essential molecules in living things, and their shape affects how they work. Protein structure is described at several levels, including primary, secondary, tertiary, and quaternary structure. These levels help explain how a protein is built and how its final form supports its job.

Primary structure is the sequence of amino acids in a protein. Secondary structure forms when parts of the chain fold into regular patterns. Tertiary structure is the overall three-dimensional shape of one protein chain. Quaternary structure appears when more than one protein chain joins together to make a working protein.

The video also shows how protein structure can be represented in different ways. A simple line drawing can show the amino acid sequence. Other models can show folding and the full 3D shape. These visual forms help students compare levels of structure and see why protein shape matters.

How Protein Shape Determines Function

the periodic table and organismal elements

the-periodic-table-and-organismal-elements

Elements in the Human Body and Periodic Table

Elements are the smallest units of matter that cannot be broken down further by chemical processes. Scientists know 118 elements, but not all of them occur naturally. Only a small number are essential for life, and living matter depends mostly on carbon, nitrogen, hydrogen, and oxygen. The periodic table organizes elements by their physical and chemical properties. Each square shows the element name, chemical symbol, atomic number, and atomic weight. The atomic number is the number of protons...

functional groups

Functional Groups in Organic Molecules

Functional groups are the part of an organic molecule that gives it specific chemical behavior. They help explain why compounds with similar carbon skeletons can react in different ways. In organic chemistry, these groups are often used to classify compounds. A functional group can change the properties of a molecule and affect how it behaves in a reaction. Knowing functional groups helps students recognize patterns in organic compounds. It also makes it easier to compare molecules that share...

types of chemical bonds

Chemical Bonds and How Atoms Join

Chemical bonds hold atoms together and help explain how different substances form. In chemistry, the main bond types are ionic bonds, covalent bonds, and metallic bonds. Ionic bonds form when electrons move from one atom to another. Covalent bonds form when atoms share electrons. Metallic bonds occur in metals, where electrons are held in a shared arrangement that gives metals their characteristic behavior. Understanding these bond types helps students compare how atoms connect in different...

noncovalent attractions in biomolecules

Biomolecule Interactions Without Covalent Bonds

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polymers

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chemistry of carbohydrates

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protein and protein structures

Proteins are essential molecules in living things, and their shape affects how they work. Protein structure is described at several levels, including primary, secondary, tertiary, and quaternary structure. These levels help explain how a protein is built and how its final form supports its job. Primary structure is the sequence of amino acids in a protein. Secondary structure forms when parts of the chain fold into regular patterns. Tertiary structure is the overall three-dimensional shape of...

ph regulation in cells

Cell pH and Organelle Balance

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chemistry of the cell

Cell Chemistry: Water, Ions, and Molecules

Cell chemistry explains the substances that make cells work. Water is the main component of cells, and it supports the chemical reactions that keep life going. Cells also contain organic molecules, which are carbon-based compounds, and inorganic ions, which are charged particles needed for cell function. Organic molecules in cells include carbohydrates, lipids, proteins, and nucleic acids. These molecules have different roles, but together they build cell structures, store energy, and carry...

key terms and concepts

Learn how proteins are built and folded through primary, secondary, tertiary, and quaternary structure, and how protein shape affects function.

How Protein Shape Determines Function | 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.

Florida Department of Education

SC.912.L.18

SC.912.L.18.1

SC.912.L.18.4

new-york-state-science-learning-standards

New York State Science Learning Standards

Structure and Function

HS-LS1-1.

Georgia Standards of Excellence

9-12

Biology

SB6.c

Characteristics of Life

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

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Cell Structure

Background
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Visualizing Onion and Cheek Cells
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Visualizing Onion and Human Cells
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What are Cells?

Cell Diversity

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Cytoplasm

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The Nucleus

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The Central Dogma

The DNA Helix

Nucleic Acids

DNA as a Genetic Template

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Chromosome Structure

Base-pairing and DNA Repair

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RNA Structure

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Protein Families

Types of RNA

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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

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

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Protein-Protein Interfaces

Protein Folding

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

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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

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Animal and Plant Cell Structure

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Structural Organization of the Human Body: An Overview

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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

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Accessory Organs

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Lipid Digestion

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Protein Digestion

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Carbohydrate Digestion

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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

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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

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Fertilization

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An Introduction to the Zebrafish: Danio rerio

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Physiology of the Circulatory System

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Anatomy of the Circulatory System

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Anatomy of the Heart

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Measuring Circulatory System Function in Humans
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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
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Kidney Structure

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Blood Withdrawal II

Source: Kay Stewart, RVT, RLATG, CMAR; Valerie A. Schroeder, RVT, RLATG. University of Notre Dame, IN
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Overview

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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.]

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How Protein Shape Determines Function

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