Detailed Information on Publication Record
2009
Investigation of Thermal Denaturation of Barley Nonspecific Lipid Transfer Protein 1 (ns-LTP1b) by Nuclear Magnetic Resonance and Differential Scanning Calorimetry
MATEJKOVÁ, Michaela, Jitka ŽÍDKOVÁ, Lukáš ŽÍDEK, Michaela WIMMEROVÁ, Josef CHMELÍK et. al.Basic information
Original name
Investigation of Thermal Denaturation of Barley Nonspecific Lipid Transfer Protein 1 (ns-LTP1b) by Nuclear Magnetic Resonance and Differential Scanning Calorimetry
Name in Czech
Zkoumání teplotních denaturací nespecifického lipid transfer proteinu 1 (ns-LTP1b) pomocí nukleární magnetické resonance a diferenciální skenovací kalorimetrie
Authors
MATEJKOVÁ, Michaela (703 Slovakia, belonging to the institution), Jitka ŽÍDKOVÁ (203 Czech Republic, belonging to the institution), Lukáš ŽÍDEK (203 Czech Republic, guarantor, belonging to the institution), Michaela WIMMEROVÁ (203 Czech Republic, belonging to the institution), Josef CHMELÍK (203 Czech Republic) and Vladimír SKLENÁŘ (203 Czech Republic, belonging to the institution)
Edition
Journal of Agricultural and Food Chemistry, WASHINGTON, AMER CHEMICAL SOC, 2009, 0021-8561
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
21101 Food and beverages
Country of publisher
United States of America
Confidentiality degree
není předmětem státního či obchodního tajemství
Impact factor
Impact factor: 2.469
RIV identification code
RIV/00216224:14310/09:00036779
Organization unit
Faculty of Science
UT WoS
000269747500053
Keywords in English
Non-specific lipid transfer protein 1; barley grain; thermaldenaturation; nuclear magnetic resonance; differential scanningcalorimetry
Tags
International impact, Reviewed
Změněno: 9/3/2015 05:39, prof. Mgr. Lukáš Žídek, Ph.D.
V originále
Process of thermal denaturation of covalently modified form of barley grain non-specific lipid transfer protein 1b (ns-LTP1b) was investigated by nuclear magnetic resonance (NMR) and differential scanning calorimetry (DSC) up to 115\,$^\circ$C. The denaturation was found to be irreversible and highly cooperative. A method of numerical quantitative analysis allowing to fit the NMR data to a transition-state model without further simplification was developed. Based on the obtained values of transition state enthalpy and entropy, rate of denaturation was calculated as a simple measure of protein stability at various temperatures. 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.
In Czech
Process of thermal denaturation of covalently modified form of barley grain non-specific lipid transfer protein 1b (ns-LTP1b) was investigated by nuclear magnetic resonance (NMR) and differential scanning calorimetry (DSC) up to 115\,$^\circ$C. The denaturation was found to be irreversible and highly cooperative. A method of numerical quantitative analysis allowing to fit the NMR data to a transition-state model without further simplification was developed. Based on the obtained values of transition state enthalpy and entropy, rate of denaturation was calculated as a simple measure of protein stability at various temperatures. 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.
Links
LC06030, research and development project |
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MSM0021622413, plan (intention) |
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