Morphology and the strength of intermolecular contacts in protein crystals.

Morphology and the strength of intermolecular contacts in protein crystals.
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蛋白质晶体的形态和分子间接触的强度。

DOI:
10.1107/s0907444903011107
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发表时间:
2003
期刊:
Acta crystallographica. Section D, Biological crystallography
影响因子:
--
通讯作者:
A. Chernov
A. Chernov
中科院分区:
--
文献类型:
--
作者:
Y. Matsuura;A. Chernov

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在溶菌酶晶体的四种多态修饰中,基于分子间原子对之间的键强度,估计了分子间接触(大键)的强度和每个接触在分子表面上所占的面积。研究表明,这些大键的周期性键链决定了蛋白质晶体的形态。库仑对宏观键强度的贡献也进行了估计。利用接触强度并考虑键水化作用,估计了不同晶面的晶体-水界面能。所有接触的区域都映射到分子表面,利用接触的极坐标表示。比较不同多晶修饰下分子间接触的位置,发现这些接触可以在分子表面形成各种各样的斑块。除了凹面活性部位的内部外,这些斑块几乎位于表面的任何地方。研究还表明,经常涉及水分子的接触是在非特异性吸引静电相互作用的背景下由特定的分子间氢键形成的。将典型的大键强度值与其他蛋白质复合物系统中的结合强度进行了比较。
The strengths of intermolecular contacts (macrobonds) and the areas occupied by each contact on the molecular surface were estimated in four polymorphic modifications of lysozyme crystals based on the bond strengths between individual atomic pairs belonging to the molecules in contact. It has been shown that the periodic bond chains of these macrobonds account for the morphology of protein crystals. The Coulombic contribution to the macrobond strength has also been estimated. Making use of the contact strengths and taking into account bond hydration, crystal-water interfacial energies were also estimated for different crystal faces. The areas of all contacts are mapped on the molecular surface, making use of a polar-coordinate representation of the contact. Comparing the locations of the intermolecular contacts in the different polymorphic crystal modifications, it is shown that these contacts can form a wide variety of patches on the molecular surface. The patches are located practically everywhere on the surface except for the inside of a concave active site. It is also shown that the contacts, which frequently involve water molecules, are formed by specific intermolecular hydrogen bonds on a background of non-specific attractive electrostatic interactions. Typical values of the macrobond strength are compared with the strength of association in other protein-complex systems.
DOI: 10.1021/bi00507a030
发表时间: 1981-01-01
期刊: BIOCHEMISTRY
影响因子: 2.9
作者:
WOLFENDEN, R;ANDERSSON, L;SOUTHGATE, CCB
通讯作者: SOUTHGATE, CCB
DOI: 10.1016/s0022-2836(05)80364-x
发表时间: 1990-10-05
影响因子: 5.6
作者:
IPPOLITO, JA;ALEXANDER, RS;CHRISTIANSON, DW
通讯作者: CHRISTIANSON, DW