Possible manifestations of variations in the tertiary structure of proteins in vibrational spectra are considered. The study is based on the assumption that normal modes of vibrations of structural elements of protein molecules must contribute to Raman and/or FTIR spectra. Vibrational modes of large fragments corresponding to higher levels of hierarchy of protein structure must be observed in the low-frequency (50-500 cm⁻¹) spectral interval. Fingerprint-range and low-frequency Raman and FTIR spectra of structurally different proteins (collagen, gelatin, chymotrypsin, and albumin) and polypeptide (poly-l-lysine in two conformations) are studied. Spectra of native and thermally denatured proteins are compared. Several spectral features that may correspond to the tertiary structure are considered.

考虑了振动光谱中蛋白质三级结构变化的可能表现。该研究基于以下假设：蛋白质分子结构元素的正常振动模式必须对拉曼光谱和/或FTIR光谱有贡献。必须在低频（50-500 cm ^-1）光谱区间内观察到较大片段的振动模式，该振动模式对应于更高层次的蛋白质结构。指纹范围和结构上不同的蛋白质的低频拉曼和红外光谱（胶原，明胶，胰凝乳蛋白酶，和白蛋白）和多肽（聚升-赖氨酸有两个构象）。比较天然和热变性蛋白质的光谱。考虑了可能对应于三级结构的几个光谱特征。