Tools for Characterizing Proteins: Circular Variance, Mutual Proximity, Chameleon Sequences, and Subsequence Propensities

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

Abstract

For the characterization of various aspects of protein structures, four useful concepts are discussed: chameleon sequences, circular variance, mutual proximity, and a subsequence-based foldability score. These concepts were used in estimating foldability of globular, intrinsically disordered and fold-switching proteins, properties of protein–protein interfaces, quantifying sphericity, helping to improve protein–protein docking scores, and estimating the effect of mutations on stability. A conjecture about the Achilles’ heel of proteins is presented as well.

Original languageEnglish
Title of host publicationMethods in Molecular Biology
PublisherHumana Press Inc.
Pages39-61
Number of pages23
DOIs
StatePublished - 2022

Publication series

NameMethods in Molecular Biology
Volume2405
ISSN (Print)1064-3745
ISSN (Electronic)1940-6029

Keywords

  • Amino acid propensity
  • Chameleon sequence
  • Circular variance
  • Foldability score
  • Mutual proximity

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