title: Investigation of thermal denaturation of barley nonspecific lipid transfer protein 1 (ns-LTP1b) by nuclear magnetic resonance and differential scanning calorimetry.
abstract: 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.
authors.affiliation: National Centre for Biomolecular Research, Masaryk University, Kotlárská 2, 611 37 Brno, Czech Republic.
authors.forename: Michaela
authors.initials: M
authors.lastname: Matejková
authors.forename: Jitka
authors.initials: J
authors.lastname: Zídková
authors.forename: Lukás
authors.initials: L
authors.lastname: Zídek
authors.forename: Michaela
authors.initials: M
authors.lastname: Wimmerová
authors.forename: Josef
authors.initials: J
authors.lastname: Chmelík
authors.forename: Vladimír
authors.initials: V
authors.lastname: Sklenár
mesh_terms: 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
chemical_list: D002352:Carrier Proteins; D010940:Plant Proteins