Repeats in S1 Proteins: Flexibility and Tendency for Intrinsic Disorder.

ABSTRACT: An important feature of ribosomal S1 proteins is multiple copies of structural domains in bacteria, the number of which changes in a strictly limited range from one to six. For S1 proteins, little is known about the contribution of flexible regions to protein domain function. We exhaustively studied a tendency for intrinsic disorder and flexibility within and between structural domains for all available UniProt S1 sequences. Using charge-hydrophobicity plot cumulative distribution function (CH-CDF) analysis we classified 53% of S1 proteins as ordered proteins; the remaining proteins were related to molten globule state. S1 proteins are characterized by an equal ratio of regions connecting the secondary structure within and between structural domains, which indicates a similar organization

SUBMITTER: Machulin A 

PROVIDER: S-EPMC6566611 | biostudies-literature | 2019 May

REPOSITORIES: biostudies-literature