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dc.contributor.authorWright, Peter E.
dc.contributor.authorLerner, Richard A.
dc.contributor.authorDyson, H. Jane
dc.date.accessioned2023-10-25T11:53:26Z
dc.date.available2023-10-25T11:53:26Z
dc.date.issued1988
dc.date.submitted2023-10-25
dc.identifier.citationAdvances in protein design, 13 - 19en_US
dc.identifier.isbn0895739534
dc.identifier.isbn3527280243
dc.identifier.issn0930-4320
dc.identifier.urihttp://hdl.handle.net/10033/623514
dc.description.abstractIt is generally accepted that protein folding proceeds via local folded intermediates which function as initiation sites for cooperative growth. However, direct experimental identification of the transient early folding intermediates of native proteins is difficult because, under conditions which favor folding, the polypeptide chain folds rapidly and cooperatively into its native globular conformation. Recent developments in two-dimensional NMR spectroscopy have provided very sensitive methods for the detection of folded structures in peptide fragments of proteins in water solution. NMR experiments have provided unequivocal evidence for the formation of #-turns, nascent helix and a-helix in short linear peptides in water solution. By systematic variation of the amino acid sequence, information on the factors which stabilize secondary structure in small linear peptides can be obtained. The observation that peptide fragments of proteins adopt secondary structures in water solution has enormous implications for initiation of protein folding, for the mechanism of induction of protein-reactive anti-peptide antibodies and for T-cell recognition.en_US
dc.language.isoenen_US
dc.publisherGBF Gesellschaft für Biotechnologische Forschung mbH, Braunschweigen_US
dc.relation.ispartofseriesGBF monographs ; Volume 12en_US
dc.rightsAttribution-NonCommercial-ShareAlike 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.titleFOLDING OF PEPTIDE FRAGMENTS OF PROTEINS IN WATER SOLUTION: IMPLICATIONS FOR INITIATION OF PROTEIN FOLDINGen_US
dc.typeBook chapteren_US
dc.typeconference paperen_US
dc.contributor.departmentDepartment of Molecular Biology, Research Institute of Scripps Clinic La Jolla, California 92037, USAen_US
dc.identifier.journalAdvances in protein design, 1988en_US
refterms.dateFOA2023-10-25T11:53:26Z


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