Structural disorder of plasmid-encoded proteins in Bacteria and Archaea.

ABSTRACT:

Background

In the last decade and a half it has been firmly established that a large number of proteins do not adopt a well-defined (ordered) structure under physiological conditions. Such intrinsically disordered proteins (IDPs) and intrinsically disordered (protein) regions (IDRs) are involved in essential cell processes through two basic mechanisms: the entropic chain mechanism which is responsible for rapid fluctuations among many alternative conformations, and molecular recognition via short recognition elements that bind to other molecules. IDPs possess a high adaptive potential and there is special interest in investigating their involvement in organism evolution.

Results

We analyzed 2554 Bacterial and 139 Archaeal proteomes, with a total of 8,455,194 proteins for dis

SUBMITTER: Mitic NS 

PROVIDER: S-EPMC5922023 | biostudies-literature | 2018 Apr

REPOSITORIES: biostudies-literature