Evidence for water-tuned structural differences in proteins: an approach emphasizing variations in local hydrophilicity.

ABSTRACT: We present experimental evidence for the significant effect that water can have on the functional structure of proteins in solution. Human (HSA) and Bovine Serum Albumin (BSA) have an amino acid sequence identity of 75.52% and are chosen as model proteins. We employ EPR-based nanoscale distance measurements using double electron-electron resonance (DEER) spectroscopy and both albumins loaded with long chain fatty acids (FAs) in solution to globally (yet indirectly) characterize the tertiary protein structures from the bound ligands' points of view. The complete primary structures and crystal structures of HSA and as of recently also BSA are available. We complement the picture as we have recently determined the DEER-derived solution structure of HSA and here present the corresponding BSA s

SUBMITTER: Akdogan Y 

PROVIDER: S-EPMC3458090 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature