Unknown

Dataset Information

0

Comprehensive analysis of sequences of a protein switch.


ABSTRACT: Switches form a special class of proteins that dramatically change their three-dimensional structures upon a small perturbation. One possible perturbation that we explore is that of a single point mutation. Building on the pioneering experimental work of Alexander et al. (Alexander et al. PNAS, 2007; 104,11963-11968) that determines switch sequences between ? and ?+? folds we conduct a comprehensive sequence sampling by a Markov Chain with multiple fitness criteria to identify new switches given the experimental folds. We screen for switch sequences using a combination of contact potential, secondary structure prediction, and finally molecular dynamics simulations. Statistical properties of switch sequences are discussed and illustrated to be most sensitive to mutation at the N- and C- termini of the switch protein. Based on this analysis, a particularly stable putative switch pair is identified and proposed for further experimental analysis.

SUBMITTER: Chen SH 

PROVIDER: S-EPMC4815306 | biostudies-literature | 2016 Jan

REPOSITORIES: biostudies-literature

altmetric image

Publications

Comprehensive analysis of sequences of a protein switch.

Chen Szu-Hua SH   Meller Jaroslaw J   Elber Ron R  

Protein science : a publication of the Protein Society 20150701 1


Switches form a special class of proteins that dramatically change their three-dimensional structures upon a small perturbation. One possible perturbation that we explore is that of a single point mutation. Building on the pioneering experimental work of Alexander et al. (Alexander et al. PNAS, 2007; 104,11963-11968) that determines switch sequences between α and α+β folds we conduct a comprehensive sequence sampling by a Markov Chain with multiple fitness criteria to identify new switches given  ...[more]

Similar Datasets

| S-EPMC210043 | biostudies-other
| S-EPMC8045928 | biostudies-literature
| S-EPMC4364491 | biostudies-literature
| S-EPMC8778832 | biostudies-literature
| S-EPMC1523217 | biostudies-literature
| S-EPMC7488060 | biostudies-literature
| S-EPMC7803996 | biostudies-literature
| S-EPMC7253346 | biostudies-literature
| S-EPMC3398768 | biostudies-literature
| S-EPMC4315437 | biostudies-literature