NDLI: Truncated staphylococcal nuclease is compact but disordered.

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Truncated staphylococcal nuclease is compact but disordered.

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Truncated staphylococcal nuclease is compact but disordered.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Flanagan, J. M. Engelman, D. M. Kataoka, M. Shortle, D.
Description	Author Affiliation: Flanagan JM ( Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511.);
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.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	2
Volume Number	89
Language	English
Publisher	National Academy of Sciences
Publisher Date	1992-02-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Micrococcal Nuclease Chemistry Circular Dichroism Magnetic Resonance Spectroscopy Protein Conformation Protein Denaturation Recombinant Proteins Scattering, Radiation Staphylococcus Enzymology Structure-Activity Relationship X-Rays Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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