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Related Concept Videos

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...
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 Folding01:22

Protein Folding

Overview
Protein Folding01:25

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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.
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Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

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Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...

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Related Experiment Video

Updated: Jul 3, 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

Extending the classical sequence-structure-function paradigm through protein dynamics and context-dependent behavior.

Timir Tripathi1, Vladimir N Uversky2, Alessandro Giuliani3

  • 1Molecular and Structural Biophysics Laboratory, Department of Zoology, School of Life Sciences, North-Eastern Hill University, Shillong, India.

FEBS Letters
|July 2, 2026
PubMed
Summary
This summary is machine-generated.

Many proteins function via dynamic conformational ensembles, not just fixed structures. This expanded model highlights sequence, dynamics, and cellular context in protein behavior and disease.

Keywords:
functional plasticityintrinsic disordermolecular flexibilityprotein dynamicsstructure–function paradigmsystems protein science

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Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
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Last Updated: Jul 3, 2026

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
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Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins
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Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • The traditional paradigm links protein function to stable structures.
  • Intrinsically disordered proteins challenge this by functioning through dynamic states.
  • Evidence suggests dynamic conformational ensembles are crucial for many biological processes.

Purpose of the Study:

  • To propose an expanded conceptual model for protein function.
  • To integrate protein dynamics and cellular context into understanding protein behavior.
  • To extend the classical sequence-structure-function paradigm.

Main Methods:

  • Review of existing literature on intrinsically disordered proteins and biomolecular condensates.
  • Conceptual framework development.
  • Analysis of protein dynamics and conformational ensembles.

Main Results:

  • Proposed model: sequence → dynamics → conformational ensembles → context-dependent behavior.
  • Demonstrated the importance of dynamic ensembles in signal integration and cellular regulation.
  • Highlighted the role of reversible, context-responsive interactions in protein assemblies.

Conclusions:

  • Protein function is better understood as a continuum, incorporating dynamics and cellular context.
  • Conformational flexibility and ensemble redistribution are key drivers of protein function.
  • This expanded view is critical for understanding protein regulation and disease mechanisms.