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Related Concept Videos

Protein Folding01:22

Protein Folding

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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...
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Globular and Fibrous Proteins02:21

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Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
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Protein and Protein Structure02:15

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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.
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Related Experiment Video

Updated: May 9, 2026

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
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β-Bulges: extensive structural analyses of β-sheets irregularities.

Pierrick Craveur1, Agnel Praveen Joseph, Joseph Rebehmed

  • 1INSERM, U665, DSIMB, F-75739, Paris, France; University of Paris Diderot, Sorbonne Paris Cité, UMR_S 665, F-75739, Paris, France; Institut National de la Transfusion Sanguine (INTS), F-75739, Paris, France; Laboratoire d'Excellence GR-Ex, F-75739, Paris, France.

Protein Science : a Publication of the Protein Society
|August 2, 2013
PubMed
Summary
This summary is machine-generated.

Beta-bulges, protein structure irregularities, are common but not conserved across evolution. This study analyzed their distribution and amino acid preferences using a large dataset and molecular dynamics.

Keywords:
beta-sheetsbeta-strandevolutionfoldsminingprotein blocksprotein structurestructural alphabetstructural comparisonstructural irregularity

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Last Updated: May 9, 2026

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

Area of Science:

  • Structural Biology
  • Protein Science
  • Bioinformatics

Background:

  • Beta-sheets are fundamental protein structures stabilized by hydrogen bonds.
  • Beta-bulges are common irregularities within beta-sheets, disrupting regular patterns and affecting protein structure and function.
  • Previous research suggested potential evolutionary conservation of beta-bulges, but studies were limited in scope.

Purpose of the Study:

  • To comprehensively analyze the distribution and conservation of beta-bulges in protein structures.
  • To investigate amino acid preferences and local backbone conformations associated with beta-bulges.
  • To explore the evolutionary conservation and sequence displacement of beta-bulges.

Main Methods:

  • Analysis of a large dataset of beta-bulges, significantly larger than previous studies.
  • Characterization of local backbone conformations using a structural alphabet.
  • Investigation of amino acid composition and preferences within beta-bulges.
  • Molecular Dynamics simulations to study sequence displacement of beta-bulges.

Main Results:

  • Beta-bulges are frequently found at the N- and C-termini of beta-strands.
  • Novel amino acid preferences associated with beta-bulges were identified.
  • Contrary to previous hypotheses, no significant evolutionary conservation of beta-bulges was observed among structural homologues.

Conclusions:

  • Beta-bulges are prevalent structural motifs in proteins, with specific amino acid and local conformation preferences.
  • The study challenges the notion of significant evolutionary conservation of beta-bulges.
  • Further research using molecular dynamics provides insights into beta-bulge dynamics.