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

Durante la traducción, una cadena de aminoácidos que emergen del ribosoma forma la estructura proteica primaria. Esta cadena peptídica se mantiene unida por enlaces covalentes entre los extremos amino y carboxilo de dos aminoácidos.
Algunos aminoácidos forman enlaces de hidrógeno con sus vecinos para formar estructuras secundarias estables, como hélices alfa y láminas beta.
Las alfa-hélices son estructuras espirales unidas por enlaces de hidrógeno entre el oxígeno carbonílico y el hidrógeno amida de uno de cada cuatro residuos de aminoácidos de una cadena polipeptídica.
Las láminas beta son estructuras polipeptídicas en zigzag que se forman cuando secciones de la cadena polipeptídica interactúan lateralmente a través de enlaces de hidrógeno.
Las interacciones químicas adicionales entre las cadenas laterales de aminoácidos distantes o la columna vertebral del péptido, como las fuerzas hidrofóbicas, los enlaces iónicos y los puentes disulfuro, ayudan al polipéptido a plegarse en la estructura terciaria. Esta forma 3D es la forma funcional final de muchas proteínas.
Si dos o más cadenas polipeptídicas se combinan desde la estructura terciaria en un complejo más grande, se crea una estructura cuaternaria. Estos pueden ser complejos homoméricos o heteroméricos con funciones celulares distintas.

<ol>
	<li>Sanvictores T, Farci F. Bioquímica, Estructura Primaria de Proteínas. [Actualizado el 5 de noviembre de 2021]. En: StatPearls [Internet]. Isla del Tesoro (FL): StatPearls Publishing; 2022 Ene-. Disponible en: <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 García, Patrick L. Daubenmire, Donald J. Wink y Ginevra A. Clark. "Conectando la estructura de las proteínas con las interacciones intermoleculares: un laboratorio de modelado informático". Revista de Educación Química 93, no. 8 (2016): 1353-1363.</li>
</ol>

organización de proteínas

Las proteínas son polímeros de residuos de aminoácidos. Son versátiles y responsables de diferentes funciones celulares, incluida la replicación del ADN, el transporte molecular, la catálisis y el soporte estructural. Las proteínas tienen una estructura jerárquica que comprende al menos tres niveles de organización: estructura primaria, secundaria y terciaria. Algunas proteínas grandes tienen una estructura cuaternaria donde las subunidades proteicas individuales están unidas.

La estructura primaria de una proteína es su secuencia de aminoácidos. Los aminoácidos están unidos a través de enlaces peptídicos para formar una cadena polipeptídica con dos extremos: el extremo amino (terminal N) y el extremo carboxilo (terminal C). La secuencia de aminoácidos determina la forma plegada final de la proteína. Veinte aminoácidos diferentes están dispuestos en diferentes secuencias para crear una variedad de polipéptidos.

La estructura secundaria se refiere a regiones plegadas localmente de cadenas de aminoácidos que están estabilizadas por enlaces de hidrógeno. Hay dos tipos de estructuras secundarias: hélices alfa y láminas plegadas beta. Estos elementos estructurales secundarios están conectados por bucles simples.

A medida que las estructuras secundarias se ensamblan aún más, se genera la forma plegada final de la proteína. Esta estructura tridimensional o terciaria de una proteína se estabiliza mediante las interacciones entre las cadenas laterales de aminoácidos. Los enlaces de hidrógeno, las fuerzas electrostáticas, los enlaces disulfuro y las fuerzas de Vander Waals estabilizan la forma plegada, que suele ser el estado nativo o funcional de la proteína.

Cuando dos o más cadenas polipeptídicas plegadas llamadas subunidades proteicas forman un complejo, se crea una estructura proteica cuaternaria.

Organización de proteínas

Las proteínas son polímeros de residuos de aminoácidos. Son versátiles y responsables de diferentes funciones celulares, incluida la replicación ...

Education

Educación

JoVE Core

Cell Biology

Biología Celular

Unit 1

Unidad 1

Protein Structure

Estructura de las proteínas

KEY TERMS AND CONCEPTS

TÉRMINOS Y CONCEPTOS CLAVE

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 Biología Celular ilustra procesos celulares complejos mediante completos vídeos animados fáciles de entender. Esta colección se centra en los componentes esenciales de las células y su funcionamiento, incluyendo los orgánulos y las membranas, el transporte celular y el metabolismo energético celular. Todo este material se complementa con los vídeos de científicos en acción, que muestran la aplicación de la biología celular en experimentos reales de investigación.

Characteristics of Life

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HS-LS1-2

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HS-LS1-3

Protein Folding Levels and Bonds

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