Investigation of thermal denaturation of barley nonspecific lipid transfer protein 1 (ns-LTP1b) by nuclear magnetic resonance and differential scanning calorimetry
Language English Country United States Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
19719083
DOI
10.1021/jf902580f
Knihovny.cz E-resources
- MeSH
- Protein Denaturation * MeSH
- Calorimetry, Differential Scanning MeSH
- Hordeum chemistry MeSH
- Magnetic Resonance Spectroscopy MeSH
- Plant Proteins chemistry MeSH
- Seeds chemistry MeSH
- Carrier Proteins chemistry MeSH
- Hot Temperature * MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Plant Proteins MeSH
- Carrier Proteins MeSH
The process of thermal denaturation of a covalently modified form of barley grain nonspecific lipid transfer protein 1b (ns-LTP1b) was investigated by nuclear magnetic resonance (NMR) and differential scanning calorimetry up to 115 degrees C. The denaturation was found to be irreversible and highly cooperative. A method of numerical quantitative analysis allowing us to fit the NMR data to a transition state model without further simplification was developed. On the basis of the obtained values of transition state enthalpy and entropy, the rate of denaturation was calculated as a simple measure of protein stability at various temperatures. The effect of disulfide bond reduction on thermal denaturation of ns-LTP1b was studied and discussed in the context of quality control of barley products during storage and processing.
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