Sikorski A, Romiszowski P
Department of Chemistry, University of Warsaw, Poland.
Acta Biochim Pol. 2001;48(1):77-81.
Properties of a simple model of polypeptide chains were studied by the means of the Monte Carlo method. The chains were built on the (310) hybrid lattice. The residues interacted with long-range potential. There were two kinds of residues: hydrophobic and hydrophilic forming a typical helical pattern -HHPPHPP-. Short range potential was used to prefer helical conformations of the chain. It was found that at low temperatures the model chain formes dense and partially ordered structures (non-unique). The presence of the local potential led to an increase of helicity. The effect of the interplay between the two potentials was studied. After the collapse of the chain further annealing caused rearrangement of helical structures. Dynamic properties of the chain at low temperature depended strongly on the local chain ordering.
通过蒙特卡罗方法研究了多肽链简单模型的性质。这些链构建在(310)混合晶格上。残基通过长程势相互作用。存在两种残基：疏水和亲水的，形成典型的螺旋模式-HHPPHPP-。短程势用于优先形成链的螺旋构象。发现低温下模型链形成致密且部分有序的结构（不唯一）。局部势的存在导致螺旋度增加。研究了两种势之间相互作用的影响。链塌缩后进一步退火导致螺旋结构重排。低温下链的动力学性质强烈依赖于局部链序。
