Pressure effects on ligand binding kinetics and the heme environment in myoglobin

被引:0
作者
Schulte, A [1 ]
Galkin, O [1 ]
机构
[1] Univ Cent Florida, Dept Phys, Orlando, FL 32816 USA
来源
ADVANCES IN HIGH PRESSURE BIOSCIENCE AND BIOTECHNOLOGY II, PROCEEDINGS | 2003年
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中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The multistep kinetics of ligand binding to myoglobin is investigated at variable pressure (0.1 - 190 MPa) and temperature (180 - 300 K). The amplitude of the geminate rebinding process increases with pressure corresponding to a smaller escape fraction of ligands into the solvent. High pressures may alter the accessibility of internal cavities in the protein and specific ligand pathways.
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页码:121 / 124
页数:4
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