PRIMARY STRUCTURE EFFECTS ON PEPTIDE GROUP HYDROGEN-EXCHANGE
PRIMARY STRUCTURE EFFECTS ON PEPTIDE GROUP HYDROGEN-EXCHANGE
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DOI：
10.1002/prot.340170110
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发表时间：
1993-09-01
期刊：
影响因子：
--
通讯作者：
ENGLANDER, SW
中科院分区：
文献类型：
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作者：
BAI, YW;MILNE, JS;ENGLANDER, SW
肽基团NH氢与水溶剂氢的交换速率对相邻侧链敏感。为了评估蛋白质侧链的影响，使用二肽模型研究了所有20种天然存在的氨基酸。诱导和位阻效应都很明显。最近邻阻断和诱导效应的加和性在寡聚物和多肽中进行了测试，并且令人惊讶地得到了证实。测定了含丙氨酸肽的参考速率，并考虑了温度的影响。这些结果提供了必要的信息，以评估测量的蛋白质NH到ND的交换率，通过比较它们与预期的速率相同的氨基酸序列是非结构化的寡肽和多肽。这种方法的蛋白质研究的应用进行了讨论。(C)1993 Wiley-Liss，Inc.
The rate of exchange of peptide group NH hydrogens with the hydrogens of aqueous solvent is sensitive to neighboring side chains. To evaluate the effects of protein side chains, all 20 naturally occurring amino acids were studied using dipeptide models. Both inductive and steric blocking effects are apparent. The additivity of nearest-neighbor blocking and inductive effects was tested in oligo- and polypeptides and, surprisingly, confirmed. Reference rates for alanine-containing peptides were determined and effects of temperature considered. These results provide the information necessary to evaluate measured protein NH to ND exchange rates by comparing them with rates to be expected for the same amino acid sequence is unstructured oligo- and polypeptides. The application of this approach to protein studies is discussed. (C) 1993 Wiley-Liss, Inc.