Exploring Protein Conformational Diversity.

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ID: 74955
2019
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Ranked #72 of 139 articles by views in methods in molecular biology (clifton, nj)

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Abstract
The native state of proteins is composed of conformers in dynamical equilibrium. In this chapter, different issues related to conformational diversity are explored using a curated and experimentally based database called CoDNaS (Conformational Diversity in the Native State). This database is a collection of redundant structures for the same sequence. CoDNaS estimates the degree of conformational diversity using different global and local structural similarity measures. It allows the user to explore how structural differences among conformers change as a function of several structural features providing further biological information. This chapter explores the measurement of conformational diversity and its relationship with sequence divergence. Also, it discusses how proteins with high conformational diversity could affect homology modeling techniques.
Reference Key
monzon2019exploringmethods Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Monzon, Alexander Miguel;Fornasari, Maria Silvina;Zea, Diego Javier;Parisi, Gustavo;
Journal methods in molecular biology (clifton, nj)
Year 2019
DOI
10.1007/978-1-4939-8736-8_20
URL
Keywords
protein dynamics codnas database conformational diversity conformers native state protein evolution

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