Exploring conformational diversity using CoDNaS database

MONZON, ALEXANDER M; MARIA SILVINA FORNASARI; ZEA, DIEGO JAVIER; GUSTAVO PARISI

Methods in Molecular Biology Series Springer

Springer

Año: 2019; p. 353 - 365

The native state of proteins is composed of conformers in dynamical equilibrium. In this chapter, differentissues related to conformational diversity are explored using a curated and experimentally based databasecalled CoDNaS (Conformational Diversity in the Native State). This database is a collection of redundantstructures for the same sequence. CoDNaS estimates the degree of conformational diversity using differentglobal and local structural similarity measures. It allows the user to explore how structural differencesamong 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 sequencedivergence. Also, it discusses how proteins with high conformational diversity could affect homologymodeling techniques.