Analysis of Tandem Repeat Protein Folding Using Nearest-Neighbor Models.

ABSTRACT: Cooperativity is a hallmark of protein folding, but the thermodynamic origins of cooperativity are difficult to quantify. Tandem repeat proteins provide a unique experimental system to quantify cooperativity due to their internal symmetry and their tolerance of deletion, extension, and in some cases fragmentation into single repeats. Analysis of repeat proteins of different lengths with nearest-neighbor Ising models provides values for repeat folding ([Formula: see text]) and inter-repeat coupling (ΔG_i-1,i). In this article, we review the architecture of repeat proteins and classify them in terms of ΔG_i and ΔG_i-1,i; this classification scheme groups repeat proteins according to t

SUBMITTER: Petersen M 

PROVIDER: S-EPMC8105288 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature