Direct measurement of salt-bridge solvation energies using a peptide model system: Implications for protein stability

William C. Wimley; Klaus Gawrisch; Trevor P. Creamer

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Direct measurement of salt-bridge solvation energies using a peptide model system: Implications for protein stability

机译：使用肽模型系统直接测量盐桥溶剂化能量：对蛋白质稳定性的影响

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The solvation energies of salt bridges formed between the terminal carboxyl of the host pentapeptide AcWL- X-LL and the side chains of Arg or Lys in the guest (X) position have been measured. The energies were derived from octanol-to-buffer transfer free energies determined between pH 1 and pH 9. ~13C NMR measurements show that the salt bridges form in the octanol phase, but not in the buffer phase, when the side chains and the terminal carboxyl group are charged.

机译：已经测量了在主体五肽AcWL-X-LL的末端羧基和在客人（X）位置的Arg或Lys的侧链之间形成的盐桥的溶剂化能。这些能量来自于在pH 1和pH 9之间确定的辛醇至缓冲液的转移自由能。〜13 C NMR测量表明，当侧链和末端形成时，盐桥在辛醇相中形成，而在缓冲相中不形成。羧基带电。

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《Proceedings of the National Academy of Sciences of the United States of America》 |1996年第7期|p.2985-2990|共6页
作者
William C. Wimley; Klaus Gawrisch; Trevor P. Creamer;
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收录信息美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
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正文语种 eng
中图分类自然科学总论;
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6. Direct measurement of salt-bridge solvation energies using a peptide model system: implications for protein stability. [O] . W C Wimley, K Gawrisch, T P Creamer, 1996

机译：使用肽模型系统直接测量盐桥溶剂化能量：对蛋白质稳定性的影响。
7. Direct measurement of salt-bridge solvation energies using a peptide model system: implications for protein stability. [O] . Wimley, W C, Gawrisch, K, Creamer, T P, 1996

机译：使用肽模型系统直接测量盐桥溶剂化能量：对蛋白质稳定性的影响。

Direct measurement of salt-bridge solvation energies using a peptide model system: Implications for protein stability

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