Investigation of thermal denaturation of barley nonspecific lipid transfer protein 1 (ns-LTP1b) by nuclear magnetic resonance and differential scanning calorimetry.
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.
Matejková
Michaela
M
National Centre for Biomolecular Research, Masaryk University, Kotlárská 2, 611 37 Brno, Czech Republic.
Zídková
Jitka
J
Zídek
Lukás
L
Wimmerová
Michaela
M
Chmelík
Josef
J
Sklenár
Vladimír
V
D002152:Calorimetry, Differential Scanning; D002352:Carrier Proteins / Q000737:chemistry*; D001467:Hordeum / Q000737:chemistry*; D006358:Hot Temperature; D009682:Magnetic Resonance Spectroscopy; D010940:Plant Proteins / Q000737:chemistry*; D011489:Protein Denaturation; D012639:Seeds / Q000737:chemistry
D002352:Carrier Proteins; D010940:Plant Proteins