【摘 要】
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In atomic force spectroscopic studies of the elastomeric protein ubiquitin,the β-strands 1-5 serve as the force clamp.Simulations show how the rupture force in the force-induced unfolding depends on t
【出 处】
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中国物理学会2011年秋季学术会议
论文部分内容阅读
In atomic force spectroscopic studies of the elastomeric protein ubiquitin,the β-strands 1-5 serve as the force clamp.Simulations show how the rupture force in the force-induced unfolding depends on the kinetics of water molecule insertion into positions where they can eventually form hydrogen bonding bridges with the backbone hydrogen bonds in the force-clamp region.The intrusion of water into this region is slowed down by the hydrophobic shielding effect of carbonaceous groups on the surface residues of β-strands 1-5,which thereby regulates water insertion prior to hydrogen bond breakage.
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