A mechanism of macroscopic (amorphous) aggregation of the tobacco mosaic virus coat protein

被引:20
作者
Rafikova, ER
Kurganov, BI
Arutyunyan, AM
Kust, SV
Drachev, VA
Dobrov, EN [1 ]
机构
[1] Moscow MV Lomonosov State Univ, AN Belozerskii Inst Phys Chem Biol, Moscow 11999, Russia
[2] Russian Acad Sci, Bach Inst Biochem, Moscow 119071, Russia
关键词
tobacco mosaic virus coat protein; aggregation; denaturation; kinetics; ionic strength;
D O I
10.1016/S1357-2725(03)00106-7
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
To gain more insight into the mechanisms of heating-induced irreversible macroscopic aggregation of the tobacco mosaic virus (TMV) coat protein (CP), the effects of pH and ionic strength on this process were studied using turbidimetry, CD spectroscopy, and fluorescence spectroscopy. At 42 degreesC, the TMV CP passed very rapidly (in less than 15 s) into a slightly unfolded conformation, presumably because heating disordered a segment of the subunit where the so-called hydrophobic girdle of the molecule resides. We suppose that the amino acid residues of this girdle are responsible for the aberrant hydrophobic interactions between subunits that initiate macroscopic protein aggregation. Its rate increased by several thousands of times as the phosphate buffer molarity was varied from 20 to 70 mM, suggesting that neutralization of strong repulsive electrostatic interactions of TMV CP molecules at high ionic strengths is a prerequisite for amorphous aggregation of this protein. (C) 2003 Elsevier Science Ltd. All rights reserved.
引用
收藏
页码:1452 / 1460
页数:9
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