PROTEIN FOLDING - EFFECT OF PACKING DENSITY ON CHAIN CONFORMATION
PROTEIN FOLDING - EFFECT OF PACKING DENSITY ON CHAIN CONFORMATION
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DOI：
10.1016/0022-2836(91)90861-y
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发表时间：
1991-05-05
影响因子：
5.6
通讯作者：
COHEN, FE
中科院分区：
文献类型：
--
作者：
GREGORET, LM;COHEN, FE
Chan，Dill最近对晶格聚合物的模拟表明，致密性可能是形成二级结构的重要驱动力。我们已经使用蛋白质的旋转异构体模型对非晶格聚合物的这一结论的稳健性进行了讨论。边界条件用于加强紧凑性，排除的体积效应被显式包含在内。在立方晶格的研究中，致密性被认为影响二级结构的含量。这种影响对于密度与天然蛋白质相当的蛋白质来说是温和的，但对于密度比天然蛋白质高约30%的链来说则是巨大的。α-螺旋结构很常见，β-Sheet结构很少见。似乎格子赋予紧凑链一种有利于β-Sheet结构的组织偏见。讨论了各种多肽链简化表示法的优缺点。
Recent lattice polymer simulations by Chan, Dill suggest that compactness may be a significant driving force in the formation of secondary structure. We have addressed the robustness of this conclusion for non-lattice polymers using a rotational isomeric model of proteins. Boundary conditions are used to enforce compactness and excluded volume effects are explicitly incorporated. As in the cubic lattice studies, compactness is seen to influence secondary structure content. This effect is modest for densities comparable to native proteins but dramatic for chains that are approximately 30% more dense than native proteins. α-Helical structure is common but β-sheet structure is rare. It appears that lattices impart to compact chains an organizational bias that favors β-sheet structure. The strengths and weakness of various simplified representations of polypeptide chains are also discussed.