Name: protein folding levels and bonds
Uploaded: 2023-04-30T10:34:07.000Z
Duration: 1 min 24 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 Organization

Podczas translacji łańcuch aminokwasów wyłaniający się z rybosomu tworzy pierwotną strukturę białka. Ten łańcuch peptydowy jest utrzymywany razem przez wiązania kowalencyjne między końcami aminowymi i karboksylowymi dwóch aminokwasów.
Niektóre aminokwasy tworzą wiązania wodorowe ze swoimi sąsiadami, tworząc stabilne struktury drugorzędowe, takie jak helisy alfa i arkusze beta.
Alfa-helisy są spiralnymi strukturami utrzymywanymi razem przez wiązania wodorowe między tlenem karbonylowym a wodorem amidowym co czwartej reszty aminokwasowej łańcucha polipeptydowego.
Arkusze beta to zygzakowate struktury polipeptydowe powstające, gdy odcinki łańcucha polipeptydowego oddziałują na boki poprzez wiązania wodorowe.
Dodatkowe interakcje chemiczne między odległymi łańcuchami bocznymi aminokwasów a szkieletem peptydowym, takie jak siły hydrofobowe, wiązania jonowe i mostki dwusiarczkowe, pomagają polipeptydowi w składaniu się w strukturę trzeciorzędową. Ten kształt 3D jest ostateczną formą funkcjonalną dla wielu białek.
Jeśli dwa lub więcej łańcuchów polipeptydowych połączy się ze struktury trzeciorzędowej w większy kompleks, powstaje struktura czwartorzędowa. Mogą to być kompleksy homomeryczne lub heteromeryczne o różnych funkcjach komórkowych.

<ol>
	<li>Sanvictores T, Farci F. Biochemia, pierwszorzędowa struktura białka. [Zaktualizowano 5 listopada 2021 r.]. W: StatPearls [Internet]. Wyspa skarbów (Floryda): Wydawnictwo StatPearls; 2022 styczeń-. Dostępne od: <a href="https://www.ncbi.nlm.nih.gov/books/NBK564343/">https://www.ncbi.nlm.nih.gov/books/NBK564343/</a></li>
	<li>Abualia, Mohammed, Lianne Schroeder, Megan Garcia, Patrick L. Daubenmire, Donald J. Wink i Ginevra A. Clark. "Łączenie struktury białka z oddziaływaniami międzycząsteczkowymi: laboratorium modelowania komputerowego." Journal of Chemical Education 93, nr 8 (2016): 1353-1363.</li>
</ol>

organizacja białek

Białka są polimerami reszt aminokwasowych. Są wszechstronne i odpowiadają za różne funkcje komórkowe, w tym replikację DNA, transport molekularny, katalizę i wsparcie strukturalne. Białka mają strukturę hierarchiczną obejmującą co najmniej trzy poziomy organizacji: strukturę pierwszorzędową, drugorzędową i trzeciorzędową. Niektóre duże białka mają strukturę czwartorzędową, w której poszczególne podjednostki białka są ze sobą połączone. Podstawową strukturą białka jest jego sekwencja aminokwasów. Aminokwasy są połączone wiązaniami peptydowymi, tworząc łańcuch polipeptydowy z dwoma końcami: końcem aminowym (koniec N) i końcem karboksylowym (koniec C). Sekwencja aminokwasów określa ostateczną zwiniętą formę białka. Dwadzieścia różnych aminokwasów ułożonych jest w różnych sekwencjach, tworząc różnorodne polipeptydy. Struktura drugorzędowa odnosi się do lokalnie złożonych regionów łańcuchów aminokwasów, które są stabilizowane wiązaniami wodorowymi. Istnieją dwa rodzaje struktur wtórnych: alfa-helisy i beta-plisowane arkusze. Te drugorzędne elementy konstrukcyjne są połączone prostymi pętlami. W miarę dalszego składania struktur drugorzędowych generowana jest ostateczna sfałdowana forma białka. Taka trójwymiarowa lub trzeciorzędowa struktura białka jest stabilizowana przez interakcje pomiędzy łańcuchami bocznymi aminokwasów. Wiązania wodorowe, siły elektrostatyczne, wiązania dwusiarczkowe i siły Vandera Waalsa stabilizują złożoną formę, która często jest natywnym lub funkcjonalnym stanem białka. Kiedy dwa lub więcej złożonych łańcuchów polipeptydowych zwanych podjednostkami białek tworzy kompleks, powstaje czwartorzędowa struktura białka.

Organizacja białek

Białka są polimerami reszt aminokwasowych. Są wszechstronne i odpowiedzialne za różne funkcje komórkowe, w tym replikację DNA, molekularne ...

Education

JoVE Core

Cell Biology

Biologia komórki

Unit 1

Jednostka 1

Protein Structure

Struktura białek

KEY TERMS AND CONCEPTS

Kluczowe terminy i pojęcia

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 C-terminus. Twenty different amino acids can be arranged in many sequences to make a wide variety of polypeptides.

The secondary structure forms when parts of the chain fold locally. These regions are stabilized by hydrogen bonds. The two main secondary structures are alpha-helices and beta-pleated sheets. Simple loops connect these folded sections.

The tertiary structure is the full three-dimensional fold of one polypeptide chain. It is stabilized by interactions between amino acid side chains. Hydrogen bonds, electrostatic forces, disulfide linkages, and Vander Waals forces help hold the folded protein in its native, functional state.

Some proteins form a quaternary structure. This happens when two or more folded polypeptide chains, called protein subunits, join together into one complex. Large proteins can use this higher level of organization to work as a unit.

Protein Folding Levels and Bonds

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

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

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...

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

Explore protein folding from amino acid sequence to alpha-helices, beta-pleated sheets, tertiary shape, and quaternary protein subunits.

Protein Folding Levels and Bonds | JoVE K12

cell biology

JoVE Core Cell Biology illustrates complex cellular processes in easy-to-understand yet comprehensive animated video lessons. This collection focuses on the essential components and functions of cells, including organelles and membranes, cellular transport, and cell energetics. It is complemented by scientist-in-action videos that demonstrate the application of cell biology in real-world research experiments.

Characteristics of Life

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Intrinsically Disordered Proteins

Ribosomes

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Protein and Protein Structures

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Proteins: From Genes to Degradation

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protein-complexes-with-interchangeable-parts

Protein Complexes with Interchangeable Parts

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HS-LS1-2

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HS-LS1-3

Protein Folding Levels and Bonds

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