High-throughput quantification of protein structural change reveals potential mechanisms of temperature adaptation in Mytilus mussels.

ABSTRACT:

Background

Temperature exerts a strong influence on protein evolution: species living in thermally distinct environments often exhibit adaptive differences in protein structure and function. However, previous research on protein temperature adaptation has focused on small numbers of proteins and on proteins adapted to extreme temperatures. Consequently, less is known about the types and quantity of evolutionary change that occurs to proteins when organisms adapt to small shifts in environmental temperature. In this study, these uncertainties were addressed by developing software that enabled comparison of structural changes associated with temperature adaptation (hydrogen bonding, salt bridge formation, and amino acid use) among large numbers of proteins from warm- and cold-adapted

SUBMITTER: Chao YC 

PROVIDER: S-EPMC7020559 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature