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• W2086910570 startingPage "6261" @default.
• W2086910570 abstract "Modern NMR methods were used to determine the secondary structure topology of the 18 kDa peptide binding domain of the chaperone protein Hsc70 in solution. This report constitutes the first experimental conformational information on this important domain of the class of Hsp70 proteins. The domain consists of two four-stranded antiparallel beta-sheets and a single alpha-helix. The topology does not resemble at all the topology observed in the human leukocyte antigen (HLA) proteins of the major histocompatibility complex. This is significant because such resemblance was predicted on the basis of limited amino acid homology, secondary structure prediction, and related function. Moreover, the exact meander-type beta-sheet topology identified in Hsc70 has to our best knowledge not been observed in any other known protein structure." @default.
• W2086910570 created "2016-06-24" @default.
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• W2086910570 creator A5035284210 @default.
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• W2086910570 date "1995-05-16" @default.
• W2086910570 modified "2023-10-03" @default.
• W2086910570 title "The Peptide-Binding Domain of the Chaperone Protein Hsc70 Has an Unusual Secondary Structure Topology" @default.
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• W2086910570 doi "https://doi.org/10.1021/bi00019a001" @default.
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• W2086910570 hasPublicationYear "1995" @default.
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