NEUTRON-DIFFRACTION ANALYSIS OF THE SOLVENT ACCESSIBLE VOLUME IN CUBIC INSULIN CRYSTALS

被引：9

作者：

BADGER, J ^{[1
]}

KAPULSKY, A ^{[1
]}

CASPAR, DLD ^{[1
]}

KORSZUN, R ^{[1
]}

机构：

[1] BROOKHAVEN NATL LAB, DEPT BIOL, UPTON, NY 11973 USA

来源：

NATURE STRUCTURAL BIOLOGY | 1995年 / 2卷 / 01期

关键词：

D O I：

10.1038/nsb0195-77

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 average-contact distance between protein and solvent surface atoms in cubic insulin crystals has been determined from two sets of 15 Angstrom resolution neutron diffraction data. A contact distance between the water hydrogen sites and the protein surface that is significantly shorter than the average protein-water oxygen contact distance implies that many water molecules are oriented with hydrogen atoms pointed towards the protein surface. The shape of the protein solvent interface is consistent with the protein envelope obtained from atomic co-ordinates.

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页码：77 / 80

页数：4

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