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Related Concept Videos

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 Folding01:22

Protein Folding

Overview
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Structural Protein Function01:56

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 such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to form...
Structural Protein Function01:56

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 such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to form...

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Related Experiment Video

Updated: May 16, 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

Comparing proteins by their internal dynamics: exploring structure-function relationships beyond static structural

Cristian Micheletti1

  • 1Scuola Internazionale Superiore di Studi Avanzati, via Bonomea 265, Trieste, Italy. michelet@sissa.it

Physics of Life Reviews
|December 4, 2012
PubMed
Summary
This summary is machine-generated.

Protein dynamics and flexibility are crucial for function and evolutionarily conserved. Comparing protein dynamics offers new ways to find relationships missed by sequence or structure analysis.

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Area of Science:

  • Biophysics
  • Structural Biology
  • Computational Biology

Background:

  • Protein function is intrinsically linked to internal dynamics, including structural fluctuations and conformational changes.
  • Functionally relevant protein flexibility and dynamics are expected to be subject to evolutionary conservation.
  • Existing sequence and structural alignment methods may not capture all protein relationships.

Purpose of the Study:

  • To review recent progress in developing and applying general methods for comparing proteins based on internal dynamics.
  • To advance the understanding of the protein structure-function relationship through dynamics-based comparisons.

Main Methods:

  • Development of general methods for comparing protein internal dynamics.
  • Application of these methods to detect protein relationships.
  • Analysis of evolutionary conservation of functionally important dynamics.

Main Results:

  • Dynamics-based protein comparisons can reveal relationships not apparent through sequence or structural alignments.
  • Evolutionary conservation patterns exist for functionally relevant protein dynamics.
  • Progress has been made in establishing robust methodologies for dynamics-based protein analysis.

Conclusions:

  • Comparing protein internal dynamics is a valuable approach for understanding protein function and evolution.
  • Dynamics-based alignments offer complementary insights to traditional methods.
  • Further development and application of these methods will enhance our understanding of protein structure-function relationships.