Related Experiment Video
Updated: Jun 20, 2026

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
Published on: July 14, 2015
Comparative analysis of rigidity across protein families
S A Wells1, J E Jimenez-Roldan, R A Römer
1Department of Physics and Centre for Scientific Computing, University of Warwick, Coventry, CV4 7AL, UK.
Abstract:
We present a comparative study in which 'pebble game' rigidity analysis is applied to multiple protein crystal structures, for each of six different protein families. We find that the main-chain rigidity of a protein structure at a given hydrogen bond energy cutoff is quite sensitive to small structural variations, and conclude that the hydrogen bond constraints in rigidity analysis should be chosen so as to form and test specific hypotheses about the rigidity of a particular protein. Our comparative approach highlights two different characteristic patterns ('sudden' or 'gradual') for protein rigidity loss as constraints are removed, in line with recent results on the rigidity transitions of glassy networks.
Related Concept Videos
Protein Families
Protein Families
Conservation of Protein Domains Over Different Proteins
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Protein Folding Quality Check in the RER
Gene Families
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...
Adaptability of Cytoskeletal Filaments

