Effect of salt concentration on the pKa of acidic residues in lysozyme

Yoshito Abe, Tadashi Ueda, Hiroki Iwashita, Yoshio Hashimoto, Hiroyuki Motoshima, Yoshitugu Tanaka, Taiji Imoto

研究成果: ジャーナルへの寄稿学術誌査読

42 被引用数 (Scopus)

抄録

We determined the pKa values of acidic residues in hen lysozyme by comparing the pH dependency of stability between wild type and mutant lysozymes in which a negative charge is eliminated. In the comparison of the stability between wild type and a mutant lysozyme, the difference in pH titration curve between them could be expressed as a two-state process involving protonation of a single acidic residue. The results strongly indicated that the Aune and Tanford theory of protein denaturation [Aune, K.C. and Tanford, C. (1969) Biochemistry 8, 4579-4585] is applicable to protein stability in solution. On the other hand, the pKa values of acidic residues in the presence of low (5 mM) or high (400 mM) salt concentration were determined by means of two-dimensional NMR. We found that the pKa values obtained from the pH dependency of stability were close to those from the NMR experiment under the high salt condition. Moreover, by comparing pKa values at high salt and low salt concentrations, we could evaluate the dependency of two electrostatic interactions (salt bridge and charge-helix dipole interaction) on salt concentration.

本文言語英語
ページ(範囲)946-952
ページ数7
ジャーナルJournal of biochemistry
118
5
DOI
出版ステータス出版済み - 10月 1995

!!!All Science Journal Classification (ASJC) codes

  • 生化学
  • 分子生物学

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