PH dependence of amide chemical shifts in natively disordered polypeptides detects medium-range interactions with ionizable residues.

ABSTRACT: A growing number of natively disordered proteins undergo a folding/binding process that is essential for their biological function. An interesting question is whether these proteins have incompletely solvated regions that drive the folding/binding process. Although the presence of predominantly hydrophobic buried regions can be easily ascertained by high-sensitivity differential scanning calorimetry analysis, the identification of those residues implicated in the burial requires NMR analysis. We have selected a partially solvated natively disordered fragment of Escherichia coli, thioredoxin, C37 (38-108), for full NMR spectral assignment. The secondary chemical shifts, temperature coefficients, and relaxation rates (R(1) and R(2)) of this fragment indicate the presence of a flexible backbo

SUBMITTER: Pujato M 

PROVIDER: S-EPMC1366825 | biostudies-literature | 2005 Nov

REPOSITORIES: biostudies-literature