Coupling protein stability and protein function in Escherichia coli CspA.


Abstract

CspA is a small protein that binds single-stranded RNA and DNA. The binding site of CspA consists of a cluster of aromatic amino acids, which form an unusually large nonpolar patch on the surface of the protein. Because nonpolar residues are generally found in the interiors of proteins, this cluster may have evolved to bind nucleic acids at the expense of protein stability. Study holds ProTherm entries: 3612, 3613, 3614, 3615, 3616, 3617, 3618, 3619, 3620, 3621, 3622, 3623, 3624, 3625, 3626, 3627 Extra Details: beta sheet; protein folding; aromatic interactions;,ssDNA and ssRNA binding

Submission Details

ID: jUzJ3DbT3

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:22 p.m.

Version: 1

Publication Details
Hillier BJ;Rodriguez HM;Gregoret LM,Fold Des (1998) Coupling protein stability and protein function in Escherichia coli CspA. PMID:9565753
Additional Information

Sequence Assay Result Units