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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 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...
Protein Folding01:22

Protein Folding

Overview
Protein Organization01:13

Protein Organization

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Related Experiment Video

Updated: Jun 14, 2026

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

A novel structural motif and structural trees for proteins containing it.

A M Kargatov1, A V Efimov

  • 1Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russia.

Biochemistry. Biokhimiia
|April 7, 2010
PubMed
Summary

Researchers analyzed novel protein structural motifs, combining beta-alpha-beta units and psi-motifs. The right-handed combination is most frequent, while the left-handed form is absent, revealing new structural insights.

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Last Updated: Jun 14, 2026

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Published on: July 8, 2025

Area of Science:

  • Structural biology
  • Protein structure analysis
  • Bioinformatics

Background:

  • Proteins fold into complex three-dimensional structures essential for their function.
  • Understanding protein structural motifs is key to deciphering protein folding and function.
  • The beta-alpha-beta unit and psi-motif are known structural elements in proteins.

Purpose of the Study:

  • To describe and analyze a novel structural motif formed by combining beta-alpha-beta units and psi-motifs.
  • To investigate the occurrence and handedness of these combined motifs in proteins.
  • To construct novel structural trees based on prevalent motif combinations.

Main Methods:

  • Analysis of 140 nonhomologous proteins.
  • Identification and classification of combined beta-alpha-beta and psi-motifs.
  • Statistical analysis of motif combinations and their handedness.
  • Construction of structural trees using common motif combinations as root structures.

Main Results:

  • A novel structural motif combining beta-alpha-beta units and psi-motifs was identified.
  • Four theoretical combinations exist, each motif having left-handed and right-handed forms.
  • 158 combinations were found in 140 proteins.
  • The right-handed psi-motif with the right-handed beta-alpha-beta unit combination is most frequent (87/158 cases).
  • The left-handed beta-alpha-beta unit and left-handed psi-motif combination was not observed.

Conclusions:

  • The study reveals specific preferences in the combination and handedness of beta-alpha-beta and psi-motifs.
  • The findings contribute to a deeper understanding of protein structural organization.
  • Novel structural trees were developed, providing a framework for further protein structure research.