Source:http://linkedlifedata.com/resource/pubmed/id/11718564
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
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| pubmed:dateCreated |
2001-11-23
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| pubmed:abstractText |
Structure formation in two species of the two-disulfide variant of hen lysozyme was investigated by means of CD spectroscopy, disulfide exchange measurement, and 1H-NMR spectroscopy. One species, 2SS [6-127, 30-115], which contained the two disulfide bonds found in the alpha-domain of authentic lysozyme, had amounts of secondary and tertiary structures, and bacteriolytic activity comparable to those of authentic lysozyme, and showed a cooperative thermal unfolding. By contrast, the other species, 2SS [64-80, 76-94], which contained the beta-domain disulfide bond as well as the inter-domain one, had a limited amount of secondary structure and little tertiary structure. Disulfide-exchange did not occur for 2SS [6-127, 30-115], whereas it occurred for 2SS [64-80, 76-94], indicating that the protein main-chain fold coupled with the formation of two disulfide bonds is relatively stable for the former variant, while unstable for the latter. 1H-NMR spectra of 2SS [6-127, 30-115] showed that native-like local environment is present within the region that corresponds to the alpha-domain, while it is absent within the region that corresponds to the beta or inter-domain. These results indicate that the alpha-domain of hen lysozyme can be an independent folding domain at equilibrium. Although the bipartite nature in the structure formation of hen lysozyme is similar to that reported for alpha-lactalbumin, differences exist between the disulfide-intermediates of the two proteins in terms of the structural domain that accomplishes tertiary structure.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Anti-Bacterial Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine,
http://linkedlifedata.com/resource/pubmed/chemical/Disulfides,
http://linkedlifedata.com/resource/pubmed/chemical/Lactalbumin,
http://linkedlifedata.com/resource/pubmed/chemical/Muramidase
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| pubmed:status |
MEDLINE
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| pubmed:month |
Nov
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| pubmed:issn |
0022-2836
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| pubmed:author | |
| pubmed:copyrightInfo |
Copyright 2001 Academic Press.
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| pubmed:issnType |
Print
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| pubmed:day |
23
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| pubmed:volume |
314
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
311-20
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:11718564-Animals,
pubmed-meshheading:11718564-Anti-Bacterial Agents,
pubmed-meshheading:11718564-Chickens,
pubmed-meshheading:11718564-Circular Dichroism,
pubmed-meshheading:11718564-Cysteine,
pubmed-meshheading:11718564-Disulfides,
pubmed-meshheading:11718564-Enzyme Stability,
pubmed-meshheading:11718564-Female,
pubmed-meshheading:11718564-Lactalbumin,
pubmed-meshheading:11718564-Magnetic Resonance Spectroscopy,
pubmed-meshheading:11718564-Micrococcus luteus,
pubmed-meshheading:11718564-Models, Molecular,
pubmed-meshheading:11718564-Muramidase,
pubmed-meshheading:11718564-Mutation,
pubmed-meshheading:11718564-Protein Denaturation,
pubmed-meshheading:11718564-Protein Folding,
pubmed-meshheading:11718564-Protein Structure, Secondary,
pubmed-meshheading:11718564-Protein Structure, Tertiary,
pubmed-meshheading:11718564-Thermodynamics
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| pubmed:year |
2001
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| pubmed:articleTitle |
Native-like tertiary structure formation in the alpha-domain of a hen lysozyme two-disulfide variant.
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| pubmed:affiliation |
Department of Biology, Kobe University, Japan. tachiban@biol.sci.kobe-u.ac.jp
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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