Interaction and binding mechanism of lipid oxidation products to sturgeon myofibrillar protein in low temperature vacuum heating conditions: Multispectroscopic and molecular docking approaches
Shi‐ke Shen, Qian‐yun Bu, Wen‐tao Yu, Yuewen Chen, Fei‐jian Liu, Zhi-wen Ding, Junlong Mao
Abstract
-sheet and a random coil of MP, imply the MP molecules to be more unfolded. Isothermal titration calorimetry and molecular docking results showed that main driving force for binding with MP was hydrogen bond, and the binding ability of malondialdehyde was superior to that of 4-hydroxy-2-nonenal. Moreover, increasing the heating temperature was beneficial to the binding reaction and intensified the conformational transition of MP. These results will provide a reference for further studies on the lipid and protein interaction of sturgeon.
Topics & Concepts
ChemistryIsothermal titration calorimetryDocking (animal)TitrationMalondialdehydeHydrogen bondBinding siteRandom coilBiophysicsCircular dichroismCrystallographyMoleculeBiochemistryPhysical chemistryOrganic chemistryOxidative stressMedicineBiologyNursingMeat and Animal Product QualityBee Products Chemical AnalysisInsect and Pesticide Research