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• W2897789555 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." @default.
• W2897789555 created "2018-10-26" @default.
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• W2897789555 date "2018-09-27" @default.
• W2897789555 modified "2023-10-06" @default.
• W2897789555 title "Exploring Protein Conformational Diversity" @default.
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• W2897789555 doi "https://doi.org/10.1007/978-1-4939-8736-8_20" @default.
• W2897789555 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30298408" @default.
• W2897789555 hasPublicationYear "2018" @default.
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