丝氨酸蛋白酶非特异性结合位点蛋白质主链的曲轴运动模型
Model for crankshaft motion of protein backbone in nonspecific binding site of serine proteases
摘要：
最近的实验发现，反平行的$β$ -片层的非特异性结合位点的丝氨酸蛋白酶的氢键变得显着更短，更强的同步催化行为的后果进行检查。我们研究了反平行$β$ -折叠中一个普通氢键转变成一个低势垒氢键对肽基曲轴运动的影响。为了这个目的，我们利用一个现实的模型，严格的微观衍生耦合相互作用的潜力和有效的现场潜力的肽链。发现表征肽链刚性的偶联相互作用是令人惊讶的弱和排斥的性质。发现有效在位电位是一个硬电位，即，比谐波更陡在普通氢键转化为低势垒氢键时，反平行$β$ -片层中相应肽基团的曲轴运动频率大致加倍。
英文摘要：
The consequences of recent experimental finding that hydrogen bonds of the anti-parallel $β$-sheet in nonspecific binding site of serine proteases become significantly shorter and stronger synchronously with the catalytic act are examined. We investigate the effect of the transformation of an ordinary hydrogen bond into a low-barrier one on the crankshaft motion a peptide group in the anti-parallel $β$-sheet. For this purpose we make use of a realistic model of the peptide chain with stringent microscopically derived coupling interaction potential and effective on-site potential. The coupling interaction characterizing the peptide chain rigidity is found to be surprisingly weak and repulsive in character. The effective on-site potential is found to be a hard one, i.e., goes more steep than a harmonic one. At transformation of the ordinary hydrogen bond into the low-barrier one the frequency of crankshaft motion of the corresponding peptide group in the anti-parallel $β$-sheet is roughly doubled.
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