Solution-phase Raman-spectroscopic studies on synthetic collagen analogs: prolyl-prolyl-glycine and (prolyl-prolyl-glycine).
Solution-phase Raman-spectroscopic studies on synthetic collagen analogs: prolyl-prolyl-glycine and (prolyl-prolyl-glycine).
复制标题
合成胶原类似物的溶液相拉曼光谱研究：脯氨酰-脯氨酰-甘氨酸和（脯氨酰-脯氨酰-甘氨酸）。
DOI：
10.1002/bip.360231218
复制
发表时间：
1984
期刊：
影响因子：
2.9
通讯作者：
Renugopalakrishnan,V
中科院分区：
文献类型：
--
作者：
Diem,M;Bhatnagar,RS;Druyan,ME;Renugopalakrishnan,V
振动光谱已被广泛用于蛋白质结构的研究14，并产生了有价值的信息内和分子间的相互作用，有助于蛋白质结构的稳定性。振动光谱技术在生物大分子结构研究中的应用在很大程度上依赖于解释所观察到的振动的分子起源的成熟的理论框架，以及使用结构良好表征的模型化合物4来简化对所观察到的光谱的分析。胶原蛋白是脊椎动物和无脊椎动物的主要结构蛋白质，目前还没有一个充分的理论背景。胶原蛋白具有独特的三螺旋结构，其中三条相互缠绕的多肽链以聚脯氨酸I1型构象存在。胶原蛋白含有比任何其他主要蛋白质更多的亚氨基残基，并且亚氨基肽键的立体化学特征和相互作用在胶原蛋白折叠的产生中起主要作用。对胶原和几种胶原样多肽的大量研究6表明，胶原中的构象决定性相互作用，如氢键，与其他蛋白质中发现的相互作用不同。（1100个残基）多肽链不均匀：事实上，基本重复Gly的某些区域-XX三肽特别富含亚氨基残基，因此可能比其他亚氨基残基稀少的区域更接近地模拟聚脯氨酸I1螺旋。我们已经调查，通过FT红外和拉曼光谱，无论是iminodeficient以及imino-rich模型肽，以确定胶原蛋白的振动光谱特征。在前一类模型化合物中，我们研究了Ala-Gly-Gly，已知其以胶原蛋白样缔合形式存在于固体中（参见参考文献7和其中引用的参考文献）。它的振动特征与在胶原中观察到的振动特征有某些相似之处。L2
Vibrational spectroscopy has been used extensively in investigations of the structure of proteins14 and has yielded valuable information on the intra-and intermolecular interactions contributing to the stability of protein structures. The application of vibrational spectroscopic techniques to structural studies on biological macromolecules has depended, to a considerable extent, on a well-developed theoretical framework explaining the molecular origin of the observed vibrations, and on the use of structurally wellcharacterized model compounds4 to simplify the analysis of the observed spectra. An adequate theoretical background has not yet been developed for collagen, the principal structural protein in vertebrates and invertebrates. Collagen has a unique triple-helical structure in which the three intertwined polypeptide chains exist in a polyproline I1 type of conformation? Collagen contains more imino residues than any other major proteins and the stereochemical characteristics and interactions of imino peptide bonds play a predominant role in the generation of the collagen fold. Numerous studies on collagen and several collagenlike polypeptides6 suggest that conformation-determining interactions, such as hydrogen bonding, in collagen are different from the interactions found in other proteins.The study of such interactions is complicated by the fact that the distribution of imino residues along the (1100 residue) polypeptide chain is not uniform: in fact, some areas of the basic repeating Gly-XX tripeptides are especially rich in imino residues and thus are likely to mimic the polyproline I1 helix more closely than other regions that are sparse in imino residues. We have investigated, via FT ir and Raman spectroscopies, both iminodeficient as well as imino-rich model peptides to identify vibrational spectral features of collagen. In the former class of model compounds, we have studied Ala-Gly-Gly, which is known to exist in the solid in a collagenlike association (see Ref. 7 and references cited therein). Its vibrational features exhibit certain similarities to the ones observed in co1lagen.% l2