NDLI: The structure of the transition state for the association of two fragments of the barley chymotrypsin inhibitor 2 to generate native-like protein: implications for mechanisms of protein folding.

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The structure of the transition state for the association of two fragments of the barley chymotrypsin inhibitor 2 to generate native-like protein: implications for mechanisms of protein folding.

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The structure of the transition state for the association of two fragments of the barley chymotrypsin inhibitor 2 to generate native-like protein: implications for mechanisms of protein folding.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	De Prat Gay, G. Ruiz-sanz, J. Fersht, A. R. Davis, B.
Description	Author Affiliation: de Prat Gay G ( Medical Research Council Unit for Protein Function and Design, University of Cambridge, United Kingdom.);
Abstract	Possible early events in protein folding may be studied by dissecting proteins into complementary fragments. Two fragments of chymotrypsin inhibitor 2 [CI2-(20-59) and CI2-(60-83)] associate to form a native-like structure in a second-order reaction that combines collision and rearrangement. The transition state of the reaction, analyzed by the protein engineering method on 17 mutants, is remarkably similar to that for the folding of the intact protein--a structure that resembles an expanded version of the folded structure with most interactions significantly weakened. The exception is that the N-terminal region of the single alpha-helix (the N-capping box) is completely formed in the transition state for association of the fragments, whereas it is reasonably well formed for the intact protein. Preliminary evidence on the structures of the individual fragments indicates that both are mainly nonnative, lacking native secondary structure and having regions of nonnative buried hydrophobic clusters. The association reaction does not result from the collision of a subpopulation of two fully native-like fragments but involves a considerable rearrangement of structure.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	23
Volume Number	91
Language	English
Publisher	National Academy of Sciences
Publisher Date	1994-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Chymotrypsin Antagonists & Inhibitors Plant Proteins Chemistry Protein Folding Serine Proteinase Inhibitors Amino Acid Sequence Circular Dichroism Hordeum Enzymology Magnetic Resonance Spectroscopy Molecular Sequence Data Mutagenesis, Site-Directed Peptides Protein Structure, Secondary Protein Structure, Tertiary Structure-Activity Relationship Thermodynamics Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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