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Related Concept Videos

Protein Organization01:13

Protein Organization

Overview
Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.
Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.
Protein Organization01:13

Protein Organization

Overview
Protein and Protein Structure02:15

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...
Protein and Protein Structures02:15

Protein and Protein Structures

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...

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Related Experiment Video

Updated: Jun 7, 2026

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
09:51

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

Structural biology. Protein structure gets exciting.

Allison Doerr

    Nature Methods
    |November 5, 2010
    PubMed
    Summary
    This summary is machine-generated.

    Researchers used nuclear magnetic resonance spectroscopy to determine the excited-state structure of a small protein. This advancement offers new insights into protein dynamics and function.

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    Last Updated: Jun 7, 2026

    Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
    09:51

    Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

    Published on: July 16, 2017

    Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry
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    Published on: January 10, 2018

    Area of Science:

    • Structural Biology
    • Biophysics
    • Spectroscopy

    Background:

    • Understanding protein structure is crucial for comprehending biological function.
    • Excited-state structures provide dynamic information beyond ground-state conformations.

    Discussion:

    • Nuclear magnetic resonance (NMR) spectroscopy is a powerful tool for atomic-level structural determination.
    • The study successfully applied NMR to probe the transient excited-state of a small protein.

    Key Insights:

    • The excited-state structure of the small protein was elucidated.
    • This provides a detailed view of protein conformation in an excited state.

    Outlook:

    • Further applications of NMR spectroscopy for studying protein dynamics.
    • Implications for drug design and understanding protein-related diseases.