Dynamics: A key to protein function

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

Proteins are complex entities created from 20 types of amino acids. The diverse functionality of proteins originates from the spatial organization of the protein chain. This brings residues that are far from sequence into proximity and enables the coordinated action of chemical groups. The cleavage of an amide bond, for example, requires an attacking nucleophile and a general acid to activate the nucleophile. Although the variety of three-dimensional architectures (i.e., folds) results in versatile functions, the static arrangement of amino acids cannot fulfill even the simplest biological activity. Binding of oxygen to hemoglobin would be hindered by steric conflicts unless protein sidechains change their position to create a free path toward the heme group.

Original languageEnglish
Title of host publicationComputational Approaches to Protein Dynamics
Subtitle of host publicationFrom Quantum to Coarse-Grained Methods
PublisherCRC Press
Pages3-38
Number of pages36
ISBN (Electronic)9781482297867
ISBN (Print)9781466561571
DOIs
Publication statusPublished - Jan 1 2014

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Chemistry(all)
  • Physics and Astronomy(all)

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  • Cite this

    Fuxreiter, M. (2014). Dynamics: A key to protein function. In Computational Approaches to Protein Dynamics: From Quantum to Coarse-Grained Methods (pp. 3-38). CRC Press. https://doi.org/10.1201/b17979