Force probing of protein crystals: An atomic force microscopy study

被引:6
|
作者
Mollica, V
Relini, A
Rolandi, R
Bolognesi, M
Gliozzi, A
机构
[1] Univ Genoa, Dept Phys, I-16146 Genoa, Italy
[2] INFM, I-16146 Genoa, Italy
[3] Adv Biotechnol Ctr, I-16132 Genoa, Italy
来源
EUROPEAN PHYSICAL JOURNAL E | 2000年 / 3卷 / 04期
关键词
D O I
10.1007/s101890070002
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 atomic force microscope (AFM) was used for measuring force-distance curves on horse spleen ferritin crystals in liquid environment. In the region of the approach curve which corresponds to tip-surface contact, discrete jumps were recorded, as predicted by molecular dynamics simulations in the case of low tip-sample interaction. The observed jumps can be related to the removal of individual molecules from the surface by the AFM tip. A simple steric model, which takes into account tip and ferritin molecule size; can explain the displacements observed with excellent agreement. The elemental force jump resulting from the approach curves is a direct measure of the force required to remove a single molecule from the crystal face. Sire discuss the conditions under which the cantilever potential energy difference along the elemental force step provides the energy of extraction of a single molecule. The estimate of the intermolecular binding energy turns out to be in good agreement with the value calculated independently from the surface free energy of ferritin crystals.
引用
收藏
页码:315 / 321
页数:7
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