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首页> 外文期刊>Journal of Theoretical Biology >A Model for Circular Dichroism Monitored Dimerization and Calcium Binding in an EF-Hand Synthetic Peptide
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A Model for Circular Dichroism Monitored Dimerization and Calcium Binding in an EF-Hand Synthetic Peptide

机译：EF手合成肽中的二向色性监测二聚和钙结合的模型。

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摘要

EF-hand peptides have been shown to bind calcium and dimerize to form an intact protein domain. A synthetic 33-residue EF-hand peptide with the sequence of carp parvalbumin CD site demonstrated a seven-fold increase in the apparent calcium dissociation constant with a eight-fold decrease in peptide concentration when fit to a single-site calcium-binding model. This observation is consistent with EF-hand dimerization. This paper describes a method to determine the dimerization dissociation constant and the calcium dissociation constants for both the monomer and dimer forms of this EF-hand peptide using circular dichroism techniques. By monitoring the increase in negative molar ellipticity at 222 nm with increasing peptide concentration under calcium-saturating conditions the dimerization dissociation constant for the synthetic parvalbumin CD site was determined to be 55.68 plus or minus 10.76 mu M. Using the dimerization constant, the calcium dissociation constants for both the monomer and dimer forms of this peptide were determined by monitoring the change in ellipticity of peptide solutions on addition of increasing amounts of calcium. A fit of this data to a mathematical model that takes into account dimerization results in calcium dissociation constants of 421.3 plus or minus 21.56 and 47.06 plus or minus 6.72 mu M for the monomer and dimer forms, respectively.
机译：EF手肽已显示结合钙并二聚形成完整的蛋白质结构域。合成的33个残基的EF手肽具有鲤鱼小白蛋白CD位点的序列，在适应单点钙结合模型时，表观钙解离常数增加了7倍，肽浓度降低了8倍。该观察结果与EF手二聚化一致。本文介绍了一种使用圆二色性技术测定该EF手肽的单体和二聚体形式的二聚解离常数和钙解离常数的方法。通过在钙饱和条件下监测随着肽浓度增加在222 nm处负摩尔椭圆率的增加，合成的小白蛋白CD位点的二聚解离常数确定为55.68正负10.76μM。使用该二聚常数，钙解离该肽的单体和二聚体形式的常数均通过监测肽溶液在添加增加量的钙时椭圆率的变化来确定。该数据与考虑了二聚化的数学模型的拟合导致单体和二聚体形式的钙解离常数分别为421.3正负21.56和47.06正负6.72μM。

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