Truncated staphylococcal nuclease is compact but disordered.

Abstract:

:Deletion of 13 amino acids from the carboxyl terminus of the 149-amino acid staphylococcal nuclease molecule results in a denatured, partly unfolded molecule that lacks persistent secondary structure but is compact under physiological conditions. Since the modification is a carboxyl-terminal deletion, it is argued that the state resembles a peptide emerging from the ribosome just before the complete folding pathway is initiated. In this paper, we characterize the molecule by nuclear magnetic resonance, circular dichroism, and small-angle x-ray scattering measurements. The truncated nuclease shows wild-type levels of activity in the presence of calcium and is found to fold into a native-like conformation in the presence of 3',5'-bisphospho-2'-deoxythymidine, a potent inhibitor. Thus, the truncated molecule retains the capacity to fold. Our results suggest that extensive solvent exclusion generates a compact polypeptide chain prior to the development of persistent secondary structural features as a protein folds during biosynthesis.

authors

Flanagan JM,Kataoka M,Shortle D,Engelman DM

doi

10.1073/pnas.89.2.748

subject

Has Abstract

pub_date

1992-01-15 00:00:00

pages

748-52

issue

2

eissn

0027-8424

issn

1091-6490

journal_volume

89

pub_type

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