Honig B, Cohen F E
Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.
Fold Des. 1996;1(1):R17-20. doi: 10.1016/S1359-0278(96)00005-3.
It is argued that the chemical nature of the polypeptide backbone is the central determinant of the three-dimensional structures of proteins. The requirement that buried polar groups form intramolecular hydrogen bonds limits the fold of the backbone to the well known units of secondary structure while the amino acid sequence chooses among the set of conformations available to the backbone. 'Sidechain-only' models, based for example on hydrophobicity patterns, fail to account for the properties of the backbone and thus will have difficulty capturing essential features of a folding pathway. This is evident from the incorrect predictions they make for the conformations of the limiting cases of all-hydrophobic or all-polar sequences.
有人认为，多肽主链的化学性质是蛋白质三维结构的核心决定因素。埋藏的极性基团形成分子内氢键的要求将主链的折叠限制在众所周知的二级结构单元中，而氨基酸序列则在主链可用的构象集合中进行选择。例如基于疏水性模式的“仅侧链”模型无法解释主链的性质，因此难以捕捉折叠途径的基本特征。这从它们对全疏水或全极性序列的极限情况构象所做的错误预测中可以明显看出。
