Experimental evaluation of the effective dielectric constant of proteins.
Experimental evaluation of the effective dielectric constant of proteins.
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DOI：
10.1016/0022-2836(80)90184-9
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发表时间：
1980-08
影响因子：
5.6
通讯作者：
D. Rees
中科院分区：
文献类型：
--
作者：
D. Rees
改变还原-氧化蛋白质中残基的净电荷的化学修饰通过改变氧化还原中心处的静电势来影响蛋白质的氧化还原电位。如果修饰电荷的位置是已知的，则氧化还原电位的偏移可以用于确定氧化还原中心和修饰残基之间的相互作用的有效介电常数。从氧化还原电位的变化后，特定的赖氨酸在hemoprotein cytochromec中的电荷中和，计算出约50的有效介电常数的修饰的赖氨酸和血红素铁在天然蛋白质之间的静电相互作用。
Chemical modifications that alter the net charge of residues in reduction-oxidation proteins influence the redox potential of the protein by changing the electrostatic potential at the redox center. If the locations of the modified charges are known, the shift in redox potential may be used to determine the effective dielectric constant for the interactions between the redox center and modified residues. From the shift in redox potential upon charge neutralization of specific lysines in the hemoprotein cytochromec, an effective dielectric constant of approximately 50 is calculated for the electrostatic interaction between the modified lysines and heme iron in the native protein.