Binding of amphiphilic peptides to a carboxy-terminal tryptic fragment of calmodulin.

Binding of amphiphilic peptides to a carboxy-terminal tryptic fragment of calmodulin.
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两亲性肽与钙调蛋白的羧基末端胰蛋白酶片段的结合。

DOI:
10.1021/bi00417a006
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发表时间:
1988
期刊:
影响因子:
2.9
通讯作者:
Puett,D
Puett,D
中科院分区:
生物学3区
文献类型:
--
作者:
Sanyal,G;Richard,LM;Carraway3rd,KL;Puett,D

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Department of Chemistry, Hamilton College, Clinton, New York 13323, andReproductive Sciences and Endocrinology Laboratories, Department of Biochemistry and Molecular Biology, University of Miami, Miami, Florida 33101 Received September 15, 1987; Revised Manuscript Received March 31, 1988 abstract: Calmodulin (CaM) fragments 1-77 (CaM 1-77) and 78-148 (CaM 78-148) were prepared by tryptic cleavage of CaM. CaM 78-148 exhibited Ca2+-dependent binding to mastoparan X, Polistes mastoparan, and melittin with apparent dissociation constants< 0.2 µ as judged from changes in the fluorescence spectrum and anisotropy of the single tryptophan residue of each of these cationic, amphiphilic peptides. This interaction was accompanied by a large spectral blue shiftof the peptide fluorescence spectrum. These findings are consistent with earlier results [Malencik, D. A., & Anderson, S. R.(1984) Biochemistry 23, 2420-2428] on the binding of mastoparan X to CaM fragment 72-148. The binding of the peptide to CaM 78-148 also caused a significant loss of the accessibility of the peptide tryptophan to the fluorescence quencher acrylamide. The CaM 78-148 induced effects on the fluorescence spectra and tryptophan ac-cessibility of the peptides were most pronounced for mastoparan X, a peptide with tryptophan on the apolar face of the putativeamphiphilic helix. The data were comparable with results from parallel experiments on the Ca2+-dependent interaction of these peptides with intact CaM. Difference circular dichroic spectra suggested that binding to CaM 78-148 was associated with the induction of considerable degrees of helicity in the amphiphilic peptides, which bythemselves have predominantly random coil structures in aqueous solution. This finding is also reminiscent of the interaction of these peptides with intact CaM. Thus, the characteristics of the high-affinity peptide binding site of CaM appear to be largely retained in CaM 78-148. CaM 1-77 exhibits a much weaker affinity (dissociation constant> 20 µ) for the mastoparans.
检测产生产生 kappa 和 lambda 轻免疫球蛋白链的集落的正常 B 细胞前体。
影响因子: 11.1
作者:
H. Sauter;C. Paige
通讯作者: C. Paige
B 细胞祖细胞在免疫球蛋白重链定型前后具有不同的生长要求
DOI: --
发表时间: 1988
影响因子: 15.3
作者:
Helmut Sauter;Christopher J Paigei
通讯作者: Christopher J Paigei
DOI: --
发表时间: 1971
影响因子: 5.4
作者:
A. Williamson
通讯作者: A. Williamson
DOI: --
发表时间: 1985-09
期刊: The American journal of pathology
影响因子: --
作者:
R. Custer;G. Bosma;M. Bosma
通讯作者: R. Custer;G. Bosma;M. Bosma
影响 B 细胞克隆形成 2,4-二硝基苯基抗体增殖的因素
DOI: --
发表时间: 1972
影响因子: 5.4
作者:
B. Askonas;A. Williamson
通讯作者: A. Williamson