Document Detail


Cold denaturation and heat denaturation of Streptomyces subtilisin inhibitor. 2. 1H NMR studies.
MedLine Citation:
PMID:  1958669     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Structural transitions of the protein Streptomyces subtilisin inhibitor (SSI) from the native state to the cold-denatured and heat-denatured states were studied by 1H NMR spectroscopy in the temperature range from -10 to 60 degrees C in the acidic pH range. Assignments of some of the 1H NMR signals of SSI in the cold-denatured and heat-denatured states were performed by a combined use of selective deuteration and site-directed mutagenesis. Throughout the pH range from 2.1 to 3.1, both transitions were cooperative and basically only three distinct spectra corresponding to structures in the cold-denatured, native, and heat-denatured states were detected. In the cold-denatured state, the side-chain signals of Met73, His106, at least one Val, and two Leu were observed at distinctly shifted positions from those for a random-coiled structure, suggesting the formation of a tertiary structure, while those of Met70, His43, and Ala2 were observed at positions for a random-coiled structure. This tertiary structure in the cold-denatured state is entirely different from that in the native state, as some amino acid residues exposed to the solvent in the native state (e.g., Met73, His106) are buried while those sequestered in the native state (e.g., His43) are exposed. In the heat-denatured state, however, most 1H NMR signals were observed at random-coiled positions, indicating that there is much less tertiary structure in the heat-denatured state than in the cold-denatured state. At pH values below 2.09, a structural transition was observed from the cold-denatured state to the heat-denatured state without passing through the native state.(ABSTRACT TRUNCATED AT 250 WORDS)
Authors:
A Tamura; K Kimura; K Akasaka
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biochemistry     Volume:  30     ISSN:  0006-2960     ISO Abbreviation:  Biochemistry     Publication Date:  1991 Nov 
Date Detail:
Created Date:  1992-01-03     Completed Date:  1992-01-03     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  11313-20     Citation Subset:  IM    
Affiliation:
Department of Chemistry, Faculty of Science, Kyoto University, Japan.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Bacterial Proteins / chemistry*
Cold Temperature
Hot Temperature
Hydrogen
Hydrogen-Ion Concentration
Magnetic Resonance Spectroscopy / methods
Models, Molecular
Protein Conformation
Protein Denaturation
Serine Proteinase Inhibitors / chemistry*
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/Serine Proteinase Inhibitors; 0/subtilisin inhibitor protein, Streptomyces; 1333-74-0/Hydrogen

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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