Investigation of thermal denaturation of barley nonspecific lipid transfer protein 1 (ns-LTP1b) by nuclear magnetic resonance and differential scanning calorimetry
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
19719083
DOI
10.1021/jf902580f
Knihovny.cz E-zdroje
- MeSH
- denaturace proteinů * MeSH
- diferenciální skenovací kalorimetrie MeSH
- ječmen (rod) chemie MeSH
- magnetická rezonanční spektroskopie MeSH
- rostlinné proteiny chemie MeSH
- semena rostlinná chemie MeSH
- transportní proteiny chemie MeSH
- vysoká teplota * MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- rostlinné proteiny MeSH
- transportní proteiny 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.
Citace poskytuje Crossref.org
