PROTEIN HYDRATION ELUCIDATED BY MOLECULAR-DYNAMICS SIMULATION

被引:236
作者
STEINBACH, PJ [1 ]
BROOKS, BR [1 ]
机构
[1] NIH, DIV COMP RES & TECHNOL, STRUCT BIOL LAB, BETHESDA, MD 20892 USA
关键词
DEVIATION FROM X-RAY CRYSTAL STRUCTURE; FLUCTUATION; DIHEDRAL TRANSITIONS; GLASS TRANSITION;
D O I
10.1073/pnas.90.19.9135
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Molecular dynamics (MD) simulations covering a wide range of hydration indicate that myoglobin is fully hydrated by 350 water molecules, in agreement with experiment. These waters, originally placed uniformly about the protein, form clusters that hydrate every charged group throughout the entire simulation. Some atoms in charged groups are hydrated by two water layers while 37% of the protein surface remains uncovered. The locations of the 350 waters are consistent with those of crystallographic waters resolved by x-ray and neutron diffraction. Hydration by 350 waters at 300 K stabilizes the conformation of carboxymyoglobin measured by x-ray diffraction throughout the entire protein, halves the rate of torsional transitions, and promotes alternative conformations for surface atoms. The glass transition observed experimentally in hydrated myoglobin near 220 K is also seen in the simulations and correlates with an increase in the number of dihedral angles undergoing transitions. The anharmonic protein motion above 220 K is enhanced by protein hydration.
引用
收藏
页码:9135 / 9139
页数:5
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