Theoretical analysis of dynamic force spectroscopy experiments on ligand-receptor complexes

被引：36

作者：

Raible, M ^{[1
]}

Evstigneev, M ^{[1
]}

Reimann, P ^{[1
]}

Bartels, FW ^{[1
]}

Ros, R ^{[1
]}

机构：

[1] Univ Bielefeld, D-33615 Bielefeld, Germany

来源：

JOURNAL OF BIOTECHNOLOGY | 2004年 / 112卷 / 1-2期

关键词：

single molecule force spectroscopy; chemical reaction kinetics;

D O I：

10.1016/j.jbiotec.2004.04.017

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

The forced rupture of single chemical bonds in biomolecular compounds (e.g. ligand-receptor systems) as observed in dynamic force spectroscopy experiments is addressed. Under the assumption that the probability of bond rupture depends only on the instantaneously acting force, a data collapse onto a single master curve is predicted. For rupture data obtained experimentally by dynamic AFM force spectroscopy of a ligand-receptor bond between a DNA and a regulatory protein we do not find such a collapse. We conclude that the above mentioned, generally accepted assumption is not satisfied and we discuss possible explanations. (C) 2004 Elsevier B.V. All rights reserved.

引用

页码：13 / 23

页数：11

共 39 条

[1] AN ATOMIC-RESOLUTION ATOMIC-FORCE MICROSCOPE IMPLEMENTED USING AN OPTICAL-LEVER [J].