以肌原纤维蛋白（MP）大分子物质为研究对象，研究低温冻藏（冻藏温度、时间和反复冻融）对蛋白质空间结构和热聚集行为的影响。首先，利用低电场核磁（NMR）和差示热量扫描仪（DSC）等技术，探讨冻藏过程中原料肉冰晶形成特点（种类、形态和分布情况）；其次，通过小角X射线散射（SXAS）、园二色谱（CD）、原子力显微镜（AFM）等技术，分析冻藏条件迫使MP分子特性（分形维数、链构象、分子间相互作用力）、空间结构（二级、三级）的变化；最后，探究MP热聚集体的结构和热特性（微观结构、粒度、Zeta电位），进一步阐明冻藏条件下MP热聚集凝胶体的形成机制。从分子水平、微观水平和宏观水平系统揭示低温冻藏胁迫MP微观结构和宏观性能变化的机理，建立冻藏处理后肌原纤维蛋白空间结构的变化与热聚集行为的关系，为提高低温贮藏肌肉蛋白的质量和精深加工、构建蛋白空间结构和功能特性之间的关系提供理论基础和技术指导。

Effects on the spatial structure and thermal aggregation behavior of myofibrillar proteins (MP) are studied under cold stress (different freezing temperatures, freezing times, and freeze-thawing cycles). Firstly, ice crystal characteristics (type, shape and distribution) of raw meat are explored during frozen storage by the nuclear magnetic resonance (NMR), and differential scanning calorimetry (DSC). Secondly, effects of freezing storage on the molecular characteristics (fractal dimension, chain conformation, intermolecular interactions) and spatial structure (secondary and tertiary structure) of MP are analyzed by small-angle X-ray scattering (SXAS), circular dichroism (CD) and atomic force microscopy (AFM). Finally, the structure and heat characteristic of MP heat aggregated gel are investigated in order to clarify the formation mechanism of MP gel. Effects of low temperature storage on microstructure and macroscopic properties of MP are illustrated for revealing the molecular mechanism. Therefore, the relationship between special structural changes and heat aggregated behavior of protein is established. The study will provide the theoretical basis and technological strategies for improving the quality of muscle protein and processing deeply under low temperature storage, and building relationships between spatial structure and functional properties of protein.