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• W1979537410 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." @default.
• W1979537410 created "2016-06-24" @default.
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• W1979537410 date "1992-01-15" @default.
• W1979537410 modified "2023-09-23" @default.
• W1979537410 title "Truncated staphylococcal nuclease is compact but disordered." @default.
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• W1979537410 doi "https://doi.org/10.1073/pnas.89.2.748" @default.
• W1979537410 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/48316" @default.
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