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Related Concept Videos

Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations 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

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Related Experiment Video

Updated: Jul 17, 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

Occurrence of protein structure elements in conserved sequence regions.

Einat Sitbon1, Shmuel Pietrokovski

  • 1Department of Molecular Genetics, Weizmann Institute of Science, Rehovot, Israel. einat.sitbon@weizmann.ac.il

BMC Structural Biology
|January 11, 2007
PubMed
Summary

Conserved protein regions show distinct structural preferences. Protein strands are more conserved than helices due to their tolerance for sequence changes, influencing protein evolution and stability.

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Last Updated: Jul 17, 2026

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
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Published on: July 14, 2015

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Area of Science:

  • Biophysics
  • Structural Biology
  • Protein Science

Background:

  • Conserved protein sequence regions are vital for identifying functionally and structurally important areas.
  • Integrated analysis of protein structure and sequence data is key to understanding these regions.

Purpose of the Study:

  • To identify the structural features of conserved protein sequence regions.
  • To understand the relationship between sequence conservation and secondary structure elements.

Main Methods:

  • Integrated analysis of large-scale protein structure and sequence data.
  • Statistical analysis of diverse protein datasets.

Main Results:

  • Protein strands are overrepresented in conserved regions, while helices and turns are underrepresented.
  • Loops show similar representation in both conserved and random regions.
  • Secondary structure elements exhibit varying tolerance to sequence changes.

Conclusions:

  • Structural constraints on secondary structure elements explain conservation patterns.
  • Strands are more conserved than helices due to their higher tolerance for sequence changes.
  • Protein evolution is linked to biophysics, thermodynamic stability, and folding, with conserved regions being key determinants of protein motifs and function.