Structure and dynamics of natural and regenerated chicken feather $\beta$-keratin were investigated by ¹³C cross-polarization (CP) magic angle spinning (MAS) solid state nuclear magnetic resonance (SSNMR) spectral analysis, ¹³C and ¹H spin-lattice relaxation time measurements, and ¹³C two dimensional phase adjusted spinning sidebands (2DPASS) MAS SSNMR measurements. Chemical shift anisotropy (CSA) parameters of both natural and regenerated chicken feather $\beta$-keratin were extracted by using 2DPASS MAS SSNMR experiment. The beauty of 2DPASS MAS SSNMR experiment is it can correlate the isotropic and anisotropic dimension with the help of shearing transformation and two dimensional Fourier Transformation. Molecular correlation time at each and every magnetically inequivalent carbon site of both natural and regenerated chicken feather $\beta$-keratin were also determined. The change in molecular dynamics of structural protein after pretreatment was monitored by 2DPASS MAS SSNMR and ¹³C relaxation measurement. This type of comprehensive study will provide the information about the interrelation between the structure and dynamics of structural protein and will also shed light in the way of developing methods for conversion of animal by-products to novel product.

天然和再生鸡毛的结构和动力学 $\beta$角蛋白通过¹³ C交叉极化（CP）幻角旋转（MAS）固态核磁共振（SSNMR）光谱分析，¹³ C和¹ H自旋晶格弛豫时间测量以及¹³ C二维相位调整的旋转进行了研究边带（2DPASS）MAS SSNMR测量。天然和再生鸡羽毛的化学位移各向异性（CSA）参数$\beta$通过2DPASS MAS SSNMR实验提取角蛋白。2DPASS MAS SSNMR实验的美丽之处在于它可以借助剪切变换和二维傅立叶变换将各向同性和各向异性维数关联起来。天然和再生鸡羽毛在每个磁不等价碳位点的分子相关时间$\beta$还确定了角蛋白。通过2DPASS MAS SSNMR和¹³ C弛豫测量监测预处理后结构蛋白的分子动力学变化。这种类型的综合研究将提供有关结构蛋白的结构与动力学之间的相互关系的信息，还将以开发方法将动物副产品转化为新产品的方式阐明。