Name: protein folding and structure
Uploaded: 2020-11-23T11:47:34.000Z
Duration: 1 min 49 s
Channel: JoVE

K12 Standards

Tennessee Academic Standards

High School

Biology

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

From Molecules to Organisms: Structures and Processes

BIO1.LS1.3

Protein Folding

- [Verteller] Na de vorming van zijn secundaire structuur, zakt een eiwit in tot een tertiaire bolvorm, een unieke en individuele 3D-opmaak die zijn functie stuurt.
 Specifieker, worden de vouwpatronen bepaald door verschillende chemische interacties.
 Ten eerste, wordt de compactheid bepaald door de hydrofobiciteit van de aminozuurzijketenen, zodat nonpolaire ketens naar binnen worden geduwd, waardoor een hydrofobe kern ontstaat die is afgescheiden van de waterige omgeving.
Zwakke vanderwaalskrachten dragen bij aan het behoud van de geclusterde kern.
 Aan de buitenkant liggen vooral de aminozuren met geladen of polaire zijketens, vrij om te interageren met water.
 Zijketens met tegengestelde ladingen kunnen ionische bindingen vormen, terwijl vergelijkbaar geladen zijdes elkaar afstoten.
Polaire zijketens kunnen waterstofbindingen vormen, zowel met water als met andere polaire moleculen.
 Tot slot, fungeren disulfidebruggen als versterking.
 Deze bindingen komen voor tussen twee aangrenzende cystinemonomeren, die sulfhydryl- of SH-groepen op hun zijketens bevatten.
De zwavel op de ene bindt zich covalent aan de andere.
 De aanwezigheid van deze chemische interacties en bindingen zorgen ervoor dat het eiwit in de meest geprefereerde vorm wordt vastgezet.

protein folding

<h4>Overzicht</h4>

Eiwitten zijn ketens van aminozuren die aan elkaar zijn gekoppeld door peptidebindingen. Na de synthese vouwt een eiwit zich in tot een driedimensionale conformatie die essentieel is voor zijn biologische functie. Interacties tussen de samenstellende aminozuren sturen de eiwitvouwing, en daarom is de eiwitstructuur voornamelijk afhankelijk van de volgorde van de aminozuren.

<h4>Eiwitstructuur is cruciaal voor de biologische functie</h4>

Eiwitten vervullen een breed scala aan biologische functies, zoals het katalyseren van chemische reacties, het bieden van immunologische verdediging, opslag, transport, cellulaire communicatie, beweging en structurele ondersteuning. De functie van een eiwit hangt grotendeels af van zijn vermogen om andere moleculen te herkennen en te binden, vergelijkbaar met een sleutel en een slot. De specifieke activiteit van elk eiwit is dus afhankelijk van zijn unieke driedimensionale architectuur.

Om functioneel te zijn, moet een eiwit zich nauwkeurig vouwen. De meeste eiwitten doorlopen verschillende tussenvormen voordat ze zich in de meest stabiele, biologisch actieve structuur vouwen. Het misvouwen van eiwitten heeft nadelige effecten op de algehele werking van de cel. Bij mensen zijn verschillende ziekten het gevolg van de ophoping van verkeerd gevouwen of ongevouwen eiwitten. Deze ziekten omvatten cystische fibrose, Alzheimer, Parkinson, ALS en de ziekte van Creutzfeldt-Jakob.

<h4>Bepalende factoren voor de eiwitstructuur</h4>

Eiwitten bestaan uit &#xE9;&#xE9;n of meer ketens van aminozuren, polypeptiden genoemd. Een polypeptide wordt gesynthetiseerd als een lineaire keten die zich snel opvouwt om een driedimensionale structuur te vormen. De termen polypeptide en eiwit worden soms door elkaar gebruikt, maar meestal wordt een gevouwen polypeptide dat een biologische functie kan vervullen een eiwit genoemd. Een eiwitstructuur wordt meestal beschreven op vier niveaus: primair, secundair, tertiair en quaternair. De meeste polypeptiden vouwen zich op tot een compacte, globulaire tertiaire structuur, zoals hemoglobine, het zuurstofdragende eiwit in het bloed. Sommige eiwitten, zoals keratine, kunnen lange vezels vormen die vaak worden aangetroffen in haar en nagels.

De sequentie van aminozuren in de polypeptideketen is de primaire bepaler van de structuur ervan. De aminozuursequentie bepaalt het type en de locatie van secundaire structuren. Bovendien wordt de algehele tertiaire structuur van een eiwit voornamelijk gestabiliseerd door chemische bindingen tussen zijketens van aminozuren&#x2014;de unieke chemische groepen die aminozuren van elkaar onderscheiden. Deze zijketens zijn positief of negatief geladen, polair ongeladen of niet-polair.

De aminozuren hebben unieke fysieke en chemische eigenschappen afhankelijk van hun zijketengroepen. Bijvoorbeeld, polaire en geladen aminozuren reageren met water om waterstofbruggen te vormen en worden hydrofiel genoemd; terwijl de niet-polaire aminozuren interacties met water vermijden en hydrofoob worden genoemd. Daarom, wanneer een eiwit zich vouwt in een cellulaire omgeving, worden de zijketens van hydrofobe aminozuren in de kern van het eiwit begraven, weg van de waterige omgeving, terwijl de zijketens van hydrofiele aminozuren op het oppervlak van het eiwit worden blootgesteld.

De dicht opeengepakte hydrofobe aminozuren in de kern van het eiwit leiden tot de vorming van zwakke Van der Waals-interacties tussen de zijketengroepen. De aanwezigheid van deze Van der Waals-krachten zorgt voor extra stabiliteit van het gevouwen eiwit. De polaire aminozuren die aan het oppervlak van het eiwit zijn blootgesteld, kunnen waterstofbruggen vormen met watermoleculen of andere polaire aminozuurzijketens. De positief en negatief geladen aminozuren bevinden zich ook aan de buitenkant van een eiwit, waar ze ionaire bindingen vormen met andere nabijgelegen, tegengesteld geladen aminozuren.

Disulfidebindingen vormen zich tussen twee sulfhydrylgroepen (SH) op het aminozuur cyste&#xEF;ne. Dit is een zeer robuuste interactie die fungeert als versteviging van het gevouwen eiwit. De aanwezigheid van disulfidebindingen vergrendelt het gevouwen eiwit in zijn meest favoriete driedimensionale conformatie. De juiste vouwing van een eiwit hangt ook af van andere factoren in de cellulaire omgeving, zoals pH, zoutconcentratie, temperatuur, enz. Verandering van de fysische en chemische omstandigheden in de omgeving van een eiwit be&#xEF;nvloedt de chemische interacties die het eiwit bij elkaar houden en kan ervoor zorgen dat het eiwit zich misvouwt of ontvouwt en zijn biologische functie verliest&#x2014;een proces dat eiwitdenaturatie wordt genoemd.

Overview

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

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Education

JoVE Core

Molecular Biology

Moleculaire biologie

Unit 1

Protein Structure

Eiwitstructuur

KEY TERMS AND CONCEPTS

BELANGRIJKE TERMEN EN CONCEPTEN

Eiwitvouwing

protein folding and structure

Protein folding is the process that gives a protein its final three-dimensional shape. That shape is essential because a protein’s structure helps determine how it works in the cell.

A folded protein is stabilized by several interactions. These include hydrogen bonds, van der Waals interactions, and disulfide bridges. Each one helps hold the protein in the correct form.

When a protein does not fold properly, its structure can change. That can affect its function and can interfere with normal cell activity. Understanding protein folding helps explain how proteins become active and why shape matters in biology.

Protein Folding and Structure

what are proteins?

Proteins, Amino Acids, and Polypeptides

Proteins are built from amino acids and form polypeptides. Amino acids are the small building blocks, and a polypeptide is a chain of amino acids joined together. This basic relationship explains how proteins are made and why their structure matters. Proteins have several important roles in living things. Some proteins help build body structures, while others carry out work inside cells. The transcript also connects proteins to enzymes, which are proteins that speed up chemical reactions.

protein organization

Protein Organization and Folding Levels

Protein organization describes how a protein is arranged at several levels. These levels help explain how a chain of amino acids becomes a working molecule. The main stages are primary, secondary, tertiary, and quaternary structure. Primary structure is the linear order of amino acids in the protein chain. Secondary structure is the first step of folding. In this stage, the chain can form patterns such as helices and sheets. Tertiary structure is the overall three-dimensional shape of one...

Protein folding is the process that gives a protein its final three-dimensional shape. That shape is essential because a protein’s structure helps determine how it works in the cell. A folded protein is stabilized by several interactions. These include hydrogen bonds, van der Waals interactions, and disulfide bridges. Each one helps hold the protein in the correct form. When a protein does not fold properly, its structure can change. That can affect its function and can interfere with normal...

conservation of protein domains over different proteins

conservation-of-protein-domains-over-different-proteins

Argonaute Protein Domains Across Species

Argonaute proteins have conserved domains that help small RNAs guide gene silencing. These proteins are found across organisms, but the number of Argonaute family members can differ from one species to another. Protein domains are small, structurally independent parts of a single amino acid chain. They can keep their shape on their own, but they may still work together with other parts of the protein. During evolution, domains can duplicate, recombine, and form new combinations. This process,...

globular and fibrous proteins

Protein Shapes: Globular vs Fibrous

Proteins can be grouped by shape into globular proteins and fibrous proteins. These two subtypes also differ in how they dissolve in water and in the jobs they do in cells and tissues. Globular proteins, also called spheroproteins, are usually round in shape. They contain a mix of amino acid types and varied primary sequences. Their shapes support many functions, including enzymes, cellular messengers, and molecular transporters. These roles often need the proteins to stay soluble in the...

intrinsically disordered proteins

Flexible Protein Regions and Binding

Intrinsically disordered proteins are proteins that do not fold into one fixed three-dimensional shape. Their flexible structure helps them work with ordered proteins to do jobs that rigid proteins cannot easily do. They are found more often in eukaryotes than in prokaryotes, and they can be fully disordered or made of both ordered and disordered regions. This lack of a rigid shape is linked to amino acid makeup. These proteins usually have many polar and charged amino acids and fewer...

protein complex assembly

How Proteins Self-Assemble in Cells

Proteins can self-assemble into working complexes inside cells. Some complexes are homomeric, which means they contain more than one copy of the same protein. Others are heteromeric, which means they are built from different protein types. Most protein complexes form through ordered self-assembly. In some cases, assembly factors help guide the proteins into the correct structure. Even in the crowded space inside a cell, proteins usually find the right partners and form functional complexes. <br...

conjugated proteins

Conjugated Proteins and Their Roles

Conjugated proteins are proteins that bond with a non-protein part. Unlike simple proteins, which contain only amino acids, these protein complexes include another chemical moiety attached covalently. That extra part can change how the protein works in the body. Nucleoproteins are conjugated proteins that contain nucleic acids. They are grouped as deoxyribonucleoproteins (DNPs) or ribonucleoproteins (RNPs). A nucleosome is a common DNP example, where nuclear DNA is associated with histone...

amyloid fibrils

Amyloid Fibrils in Brain Disease

Amyloid fibrils are clumps of misfolded proteins linked to brain disease and other disorders. In normal cells, misfolded proteins are usually refolded by chaperone proteins or broken down by the proteasome. But in some mutations or diseases, these proteins can build up into large clusters and then assemble into long fibers called fibrils. Amyloid deposits were seen as early as 1639 in the liver and spleen. In 1854, Rudolph Virchow used iodine staining, a method normally used to identify...

antibody structure

Antibody Heavy and Light Chains

Antibodies are built from heavy and light chains that work together to form a Y-shaped molecule. These chains give the antibody its basic structure and help it bind to specific targets. The two upper arms of the Y contain the variable regions, which differ from one antibody to another. These variable regions help determine which antigen, or foreign molecule, the antibody can recognize. The lower part of the antibody is the constant region. This region is more similar across antibodies and...

protein families

Protein Families and Superfamilies

Protein families are groups of homologous proteins with similar amino acid sequences and three-dimensional shapes. They often appear after gene duplication, when an extra copy of a gene is added to an organism’s genome. Mutations can then change the amino acids, as long as the protein can still be made correctly. If the new proteins keep similar amino acids in key places, their domains and overall three-dimensional structure can stay similar too. Members of the same family can share as little...

key terms and concepts

Learn how protein folding creates a protein’s final shape and how hydrogen bonds, van der Waals interactions, and disulfide bridges help stabilize it.

Protein Folding and Structure | JoVE K12

molecular biology

JoVE Core Molecular Biology showcases the molecular processes of the cell through clear and concise animated video lessons. Additionally, in scientist-in-action videos, these concepts' application is demonstrated through real experiments in modern laboratories.

Arizona Science Standards

Life Science

HS+B.L1

HS+B.L1U1.5

south-carolina-college-and-career-ready-science-standards

South Carolina College and Career Ready Science Standards

B-LS1-1.

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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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. ...

the-tree-of-life-bacteria-archaea-and-eukaryotes

The Tree of Life - Bacteria, Archaea, and Eukaryotes

Prokaryotic Cells

Prokaryotes are small unicellular organisms that include the domains &#8212; Archaea and Bacteria. Bacteria include many common microorganisms, such as ...

Introduction to Virus

Viruses are unique biological entities that blur the boundary between living and non-living systems. Although they lack cellular structure and metabolic ...

Size and Structure of Viral Genomes

Viral genomes exhibit remarkable diversity in size, structure, and composition, influencing their replication strategies and interactions with host cells. ...

Compare and contrast existing models, identify patterns, and use structural and functional evidence to analyze the characteristics of life. Engage in argument about the designation of viruses as non-living based on these characteristics.
EXPLANATION: Students begin to develop patterns of living and non-living organisms in kindergarten and build on detailed characteristics of different classifications of living organisms throughout elementary and middle school. Biology 1 discussions introduce viral particles and viral cycles, building on student understanding of living organisms to engage in an argument regarding the classification of a viral particle as either living or non-living.

BIO1.LS1.1

What are Cells?

Cells are the smallest and basic units of life, whether it is a single cell that forms the entire organism, e.g., in a bacterium, or trillions of them, ...

Eukaryotic Compartmentalization

One of the distinguishing features of eukaryotic cells is that they contain membrane-bound organelles, such as the nucleus and mitochondria, that carry ...

Eukaryotic Evolution

The endosymbiont theory is the most widely accepted theory of eukaryotic evolution; however, its progression is still somewhat debated. According to the ...

Animal and Plant Cell Structure

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Evaluate comparative models of various cell types with a focus on organic molecules that make up cellular structures.
EXPLANATION: Students explicitly discuss the structure and function of major cellular organelles in seventh grade. Building on this understanding, Biology I students should shift their focus to the different types of cells found in organisms and how the role of each cell type relates to its composition and the prevalence of different organelles within that cell. An example might include the absence (or enucleation) of the nucleus in red blood cells in mammals providing for increased levels of oxygen transport in organisms or the lack of centrioles in most neurons. Varying cell types can include both prokaryotic and eukaryotic cell types.

BIO1.LS1.2

Nucleic Acids

Nucleic acids are the most important macromolecules for the continuity of life. They carry the cell&#39;s genetic blueprint and carry instructions for its ...

The DNA Helix

Deoxyribonucleic acid, or DNA, is the genetic material responsible for passing traits from generation to generation in all organisms and most viruses. DNA ...

DNA Base Pairing

Erwin Chargaff&#x2019;s rules on DNA equivalence paved the way for the discovery of base pairing in DNA. Chargaff&#x2019;s rules state that in a ...

The Central Dogma

The central dogma explains the flow of genetic information from DNA nucleotides to the amino acid sequence of proteins.
RNA is the Missing Link Between ...

DNA Packaging

Overview

Eukaryotes have large genomes compared to prokaryotes. In order to fit their genomes into a cell, eukaryotes must pack their DNA tightly inside ...

Organization of Genes

Overview

The genomes of eukaryotes can be structured in several functional categories. A strand of DNA is comprised of genes and intergenic regions. ...

Karyotyping

Describing the number and physical features of chromosomes can reveal abnormalities that underlie genetic diseases. This description is facilitated by ...

Replication in Prokaryotes

Overview

DNA replication has three main steps: initiation, elongation, and termination. Replication in prokaryotes begins when initiator proteins bind to ...

Replication in Eukaryotes

Overview

In eukaryotic cells, DNA replication is highly conserved and tightly regulated. Multiple linear chromosomes must be duplicated with high ...

Mutations

Overview

Mutations are changes in the sequence of DNA. These changes can occur spontaneously or they can be induced by exposure to environmental factors. ...

Transcription

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

Translation

Lesson: Translation
Translation is the process of synthesizing proteins from the genetic information carried by messenger RNA (mRNA). Following ...

RNA Structure

Overview
The basic structure of RNA consists of a five-carbon sugar and one of four nitrogenous bases. Although most RNA is single-stranded, it can form ...

RNA Stability

Intact DNA strands can be found in fossils, while scientists sometimes struggle to keep RNA intact under laboratory conditions. The structural variations ...

pre-mRNA Processing

In eukaryotic cells, transcripts made by RNA polymerase are modified and processed before exiting the nucleus. Unprocessed RNA is called precursor mRNA or ...

Types of RNA

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

MicroRNAs

siRNA - Small Interfering RNAs

Small interfering RNAs, or siRNAs, are short regulatory RNA molecules that can silence genes post-transcriptionally, as well as the transcriptional ...

piRNA - Piwi-interacting RNAs

PIWI-interacting RNAs, or piRNAs, are the most abundant short non-coding RNAs. More than 20,000 genes have been found in humans that code for piRNAs while ...

CRISPR and crRNAs

Bacteria and archaea are susceptible to viral infections just like eukaryotes; therefore, they have developed a unique adaptive immune system to protect ...

lncRNA - Long Non-coding RNAs

In humans, more than 80% of the genome gets transcribed. However, only around 2% of the genome codes for proteins. The remaining part produces non-coding ...

What are Proteins?

Protein Organization

Protein Families

Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein ...

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.&#160; Although these domains are often structurally ...

Globular and Fibrous Proteins

Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular ...

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows ...

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.&#160; Most protein complexes ...

Conjugated Proteins

Simple proteins and protein complexes contain only amino acids. In contrast, many other proteins, called conjugated proteins, covalently bond with ...

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein&#39;s function.&#160; For example, enzyme activity is often regulated through a feedback mechanism where the ...

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.&#160; Under most circumstances, misfolded proteins are either refolded by chaperone proteins or ...

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand ...

Antibody Structure

Phosphorylation

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their ...

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, ...

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism&#39;s survival. Most PPIs ...

GTPases and their Regulation

Guanine nucleotide-binding proteins (G-proteins), also known as GTPases, are a superfamily of proteins that regulate many cellular processes, such as cell ...

Conserved Binding Sites

Many proteins&#8217; biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein ...

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an ...

the-equilibrium-binding-constant-and-binding-strength

The Equilibrium Binding Constant and Binding Strength

The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at ...

protein-complexes-with-interchangeable-parts

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex&#8217;s function. ...

Cofactors and Coenzymes

Mechanical Protein Functions

Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical ...

Allosteric Regulation

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures ...

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other ...

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other ...

Integrate evidence to develop a structural model of a DNA molecule. Using the model, develop and communicate an explanation for how DNA serves as a template for self-replication and encodes biological information.
EXPLANATION: Discussions of DNA in earlier grades have been limited to discussions of genes and the role of genes in the appearance and activities of an organism. Biology 1 represents a student's introduction to a molecular model of a DNA as well as the organization of DNA into genes and genes subsequently into chromosomes. Students should address interactions between genes in proteins which regulate both the shape and reproduction of DNA molecules. It is important to note that not all segments of DNA are transcribed for proteins. Portions of DNA are involved in regulating the expression of genes or affect the structure of the chromosomes (replication origin, centromeres, and telomeres).

What is the Cell Cycle?

The cell cycle refers to the sequence of events occurring throughout a typical cell&#8217;s life. In eukaryotic cells, the somatic cell cycle has two ...

Interphase

The cell cycle occurs over approximately 24 hours (in a typical human cell) and in two distinct stages: interphase, which includes three phases of the ...

The Cell Cycle Control System

Positive Regulator Molecules

Inhibition of CDK Activity

S-Cdk Initiates DNA Replication

M-Cdk Drives Transition Into Mitosis

Mitogens and the Cell Cycle

Replicative Cell Senescence

Abnormal Proliferation

cells-coordinate-growth-and-proliferation

Cells Coordinate Growth and Proliferation

Create a model for the major events of the eukaryotic cell cycle, including mitosis. Compare and contrast the rates of cell division in various eukaryotic cell types in multicellular organisms.
EXPLANATION: Students first discuss mitosis in seventh grade, specifically focusing on the role of mitosis in creating genetically identical daughter cells. Biology 1 discussions should connect a student's understanding of gene expression and protein function with the process of mitosis to explore the differentiation of cell types from otherwise identical daughter cells. Discussions should also include varying rates of mitotic division and the relationship between these rates of division and the function of specific cell types within eukaryotic organisms. Examples may include the extremely limited use of mitosis by neurons due to their interconnectedness within neural networks or the rapid rates of mitosis with growing root tips.

BIO1.LS1.6

Protein Folding and Structure

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