INTER-MOLECULAR INTERACTIONS OF GLOBULAR-PROTEINS IN THE CRYSTAL STATE

被引：7

作者：

MAKAROV, AA ^{[1
]}

MONASELIDZE, DR ^{[1
]}

ESIPOVA, NG ^{[1
]}

机构：

[1] ACAD SCI GESSR, INST PHYS, TBILISI, GEORGIA

来源：

INTERNATIONAL JOURNAL OF QUANTUM CHEMISTRY | 1979年 / 16卷 / 03期

关键词：

D O I：

10.1002/qua.560160304

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

The present work is devoted to investigation of thermal transitions in the crystals of seven proteins to compare the protein globule stability in crystal and solution. Calorimetry methods, electron and optical microscopy, as well as x‐ray diffraction studies are used. It is found that protein crystals do not melt and that the destruction of the crystal lattice is a result of protein globule denaturation within the crystal. It is demonstrated that during the heating of pepsin and DF‐trypsin crystals it is possible to observe phase transition of the first order. Equilibrium temperatures of protein denaturation in crystals and in solution coincide. The peculiarities of the crystal state are revealed in the increasing thermal transition cooperativity and the system relaxation period. Copyright © 1979 John Wiley & Sons, Inc.

引用

页码：437 / 444

页数：8

共 7 条

[1]

ANDRONIKASHVILI EL, 1972, MOLEK BIOL, V6, P915

[2]

BLUNDELL T, 1972, ADV PROTEIN CHEM, V26, P280

[3]

ESIPOVA NG, 1978, MOL BIOL+, V12, P889

[4] MICROCALORIMETRY OF THERMAL-DENATURATION OF PEPSIN AND TRYPSIN IN CRYSTAL STATE [J].