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

Les protéines sont des polymères d'acides aminés liés entre eux par des liaisons peptidiques. La plupart des protéines se replient dans des structures tridimensionnelles spécifiques pour remplir leur fonction. La structure des protéines est classée en quatre catégories:primaire, secondaire, tertiaire et quaternaire.La séquence linéaire des acides aminés dans la protéine est sa structure principale. Ces séquences sont lues dans l'ordre de synthèse des polymères, à partir du N-terminal, l'extrémité amino libre, à l'extrémité C-terminale, l'extrémité carboxyle libre. Les structures secondaires se forment par liaison hydrogène entre l'oxygène du groupe carbonyle d'un acide aminé et de l'hydrogène du groupe amino d'un autre.Les structures secondaires courantes comprennent les hélices α et les feuilles β-plissés. Celles-ci et d'autres structures de connexion, telles que les β-spires, interagissent davantage pour former la structure de protéine tridimensionnelle, connue sous le nom de structure tertiaire. La formation de la structure tertiaire se produit en raison d'interactions entre les groupes R des acides aminés.Les groupes R avec des charges opposées peuvent former des liaisons ioniques, et le soufre dans deux cystéines peut former un pont disulfure covalent. Les autres contributeurs incluent les interactions hydrophobes entre les chaînes latérales hydrophobes et les liaisons hydrogène entre les chaînes latérales polaires. De plus, certaines protéines forment des structures quaternaires, des assemblages de deux ou plus de chaînes polypeptidiques.Par exemple, l'hémoglobine est une protéine composée de quatre sous-unités, deux α et deux β. Les scientifiques peuvent utiliser la structure d'une protéine pour prédire sa fonction et son emplacement dans une cellule. Les protéines du cytoplasme cellulaire contiennent des acides aminés hydrophiles sur leurs surfaces qui interagissent avec l'eau dans le cytoplasme et ont des noyaux hydrophobes.En revanche, les protéines présentes dans les membranes cellulaires ont souvent des acides aminés hydrophobes à la surface qui interagissent avec les glycérophospholipides dans la membrane et ont des noyaux hydrophiles.

<ol>
	<li>Nelson, D. L. et Cox, M. M. (2008). Principes de biochimie de Lehninger (5e éd.). W.H. Freeman. Pages 113 à 140</li>
	<li>Structure cristalline de l’hémoglobine à l’état T avec liaison à l’oxygène aux quatre hèmes.Paoli, M., Liddington, R., Tame, J., Wilkinson, A., Dodson, G. (1996) J Mol Biol 256 : 775</li>
</ol>

protéines et structure protéique

Les protéines sont l'une des molécules organiques les plus abondantes dans les systèmes vivants et ont la gamme de fonctions la plus diversifiée de toutes les macromolécules. Les protéines peuvent être structurales, régulatrices, contractiles ou protectrices. Elles peuvent servir dans le transport, le stockage ou les membranes ; ou elles peuvent être des toxines ou des enzymes. Leurs structures, comme leurs fonctions, varient considérablement. Elles sont toutes, cependant, des polymères d'acides aminés disposés dans une séquence linéaire. 
 La forme d'une protéine est essentielle à sa fonction. Par exemple, une enzyme peut se lier à un substrat spécifique au niveau de son site actif. Si ce site actif est modifié en raison de changements locaux ou de changements dans la structure globale de la protéine, l'enzyme peut être incapable de se lier au substrat. Pour comprendre comment la protéine obtient sa forme finale ou conformation, nous devons comprendre les quatre niveaux de la structure d'une protéine : primaire, secondaire, tertiaire et quaternaire. 
 Structure primaire 
 La séquence unique des acides aminés dans une chaîne polypeptidique est sa structure primaire. Par exemple, l'hormone pancréatique insuline possède deux chaînes polypeptidiques, A et B, et elles sont reliées entre elles par des liaisons disulfure. L'acide aminé N-terminal de la chaîne A est la glycine, alors que l'acide aminé C-terminal est l'asparagine.  Les séquences d'acides aminés dans les chaînes A et B sont propres à l'insuline. 
 Le gène codant la protéine détermine en fin de compte la séquence unique pour chaque protéine. Un changement dans la séquence des nucléotides de la région codante du gène peut conduire à l'ajout d'un acide aminé différent à la chaîne polypeptidique croissante, provoquant un changement dans la structure et la fonction des protéines. Dans l'anémie falciforme, la chaîne β de l'hémoglobine a une seule substitution d'acides aminés, ce qui entraîne une modification de la structure et de la fonction de la protéine. Plus précisément, la valine dans la chaîne β remplace l'acide aminé acide glutamique. En raison de ce changement d'un acide aminé dans la chaîne, les molécules d'hémoglobine forment de longues fibres qui déforment les cellules de sang rouges biconcaves, ou en forme de disque, et qui leur font prendre une forme de croissant ou de “ faucille ”, qui obstrue les vaisseaux sanguins. Cela peut entraîner d'innombrables problèmes de santé graves tels que l'essoufflement, des étourdissements, des maux de tête et des douleurs abdominales chez les personnes touchées par cette maladie. 
 Structure secondaire 
 Le repliement local du polypeptide dans certaines régions donne lieu à la structure secondaire de la protéine. Les structures les plus courantes sont les structures d'hélices α ou de feuillets plissés β. Les deux structures maintiennent leur forme par le biais de liaisons hydrogène. Les liaisons hydrogène se forment entre l'atome d'oxygène du groupe carbonyle dans un acide aminé et un autre acide aminé qui est situé quatre acides aminés plus loin le long de la chaîne. 
 Chaque tour hélicoïdal dans une hélice alpha contient 3,6 résidus d'acides aminés. Les groupes R du polypeptide (les groupes variant) dépassent de la chaîne de l'hélice α. Dans le feuillet β, les liaisons hydrogène entre les atomes du squelette de la chaîne polypeptidique forme les "plis". Les groupes R sont fixés aux carbones et s'étendent au-dessus et au-dessous des plis. Les segments plissés s'alignent de façon parallèle ou antiparallèle les uns par rapport aux autres, et des liaisons hydrogène se forment entre l'atome d'hydrogène partiellement positif dans le groupe aminé et l'atome d'oxygène partiellement négatif dans le groupe carbonyle du squelette peptidique. Les structures de l'hélice α et du feuillet plissé β sont présentes dans la plupart des protéines globulaires et fibreuses et elles jouent un rôle structural important. 
 Structure tertiaire 
 La structure tridimensionnelle unique du polypeptide est sa structure tertiaire. Cette structure est en partie due aux interactions chimiques à l'œuvre sur la chaîne polypeptidique. Principalement, les interactions entre les groupes R créent la structure tertiaire tridimensionnelle complexe de la protéine. La nature des groupes R dans les acides aminés impliqués peut neutraliser la formation de liaisons hydrogène que nous avons décrit pour les structures secondaires standard. Par exemple, les groupes R avec des charges du même signe se repoussent les uns les autres, et ceux avec des charges de signes différents sont attirés entre eux (liaisons ioniques). Lorsque le repliement des protéines a lieu, les groupes R hydrophobes des acides aminés apolaires se trouvent à l'intérieur de la protéine, alors que les groupes R hydrophiles se trouvent à l'extérieur. Les interactions entre les chaînes latérales de cystéines forment des ponts disulfure en présence d'oxygène, la seule liaison covalente qui se forme pendant le repliement des protéines. 
 Toutes ces interactions, faibles et fortes, déterminent la forme tridimensionnelle finale de la protéine. Lorsqu'une protéine perd sa forme tridimensionnelle, elle peut ne plus être fonctionnelle. 
 Structure quaternaire 
 Dans la nature, certaines protéines se forment à partir de plusieurs polypeptides, ou sous-unités, et l'interaction de ces sous-unités forme la structure quaternaire. De faibles interactions entre les sous-unités contribuent à stabiliser la structure globale. Par exemple, l'insuline (une protéine globulaire) est associée à une combinaison de liaisons hydrogène et disulfure, ce qui la fait se coller essentiellement en forme de boule. L'insuline commence comme un seul polypeptide et perd certaines séquences internes en présence de modifications post-traductionnelles après avoir formé les ponts disulfure qui maintiennent les chaînes restantes ensemble. La soie (une protéine fibreuse), cependant, a une structure en feuillet β plissé qui est le résultat de liaisons hydrogène entre les différentes chaînes. 
 Ce texte a été adapté de<a href="https://openstax.org/books/biology-2e/pages/3-4-proteins"> Openstax, Biologie 2e, Chapitre 3.4 : Protéines</a>.

Protéines et structure protéique

Les protéines sont l’une des molécules organiques les plus abondantes dans les systèmes vivants et ont la gamme de fonctions la plus diversifiée de toutes les macromolécules. Les protéines peuvent ...

Education

Enseignement

JoVE Core

Cell Biology

Biologie cellulaire

Unit 1

Unité 1

Biochemistry of the Cell

Biochimie de la cellule

KEY TERMS AND CONCEPTS

TERMES ET CONCEPTS CLÉS

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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what are lipids?

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structure of lipids

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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 Biologie cellulaire illustre les processus cellulaires complexes dans des leçons vidéos complètes mais faciles à comprendre. Cette collection se concentre sur les composants et fonctions essentiels de la cellule ; cela inclut les organelles et les membranes ainsi que le transport et le métabolisme énergétique cellulaire. Elle est complétée par nos vidéos de scientifiques à l'action qui démontrent l'application de la biologie cellulaire dans des expériences concrètes.

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

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The Nucleus

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Intrinsically Disordered Proteins

Ribosomes

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Protein Complex Assembly

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Protein Folding

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Conserved Binding Sites

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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.]

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

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Overview of Human Digestion

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Carbohydrate Digestion

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Overview

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The Parasympathetic Nervous System

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The Sympathetic Nervous System

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Fertilization

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Physiology of the Circulatory System

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Measuring Circulatory System Function in Humans
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Blood Flow

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Blood Withdrawal I

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Blood Withdrawal II

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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.]

HS-LS1-2

How Protein Shape Determines Function

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