模型蛋白折叠中的结构域。
Domains in folding of model proteins.
作者信息
Abkevich V I, Gutin A M, Shakhnovich E I
机构信息
Department of Chemistry, Harvard University, Cambridge, Massachusetts 02138, USA.
出版信息
Protein Sci. 1995 Jun;4(6):1167-77. doi: 10.1002/pro.5560040615.
By means of Monte Carlo simulation, we investigated the equilibrium between folded and unfolded states of lattice model proteins. The amino acid sequences were designed to have pronounced energy minimum target conformations of different length and shape. For short fully compact (36-mer) proteins, the all-or-none transition from the unfolded state to the native state was observed. This was not always the case for longer proteins. Among 12 designed sequences with the native structure of a fully compact 48-mer, a simple all-or-none transition was observed in only three cases. For the other nine sequences, three states of behavior-the native, denatured, and intermediate states-were found. The contiguous part of the native structure (domain) was conserved in the intermediate state, whereas the remaining part was completely unfolded and structureless. These parts melted separately from each other.
通过蒙特卡罗模拟，我们研究了晶格模型蛋白质折叠态与非折叠态之间的平衡。氨基酸序列被设计成具有不同长度和形状的明显能量最低目标构象。对于短的完全紧凑（36聚体）蛋白质，观察到了从非折叠态到天然态的全或无转变。对于更长的蛋白质，情况并非总是如此。在12个具有完全紧凑48聚体天然结构的设计序列中，仅在3种情况下观察到简单的全或无转变。对于其他9个序列，发现了三种行为状态——天然态、变性态和中间态。天然结构（结构域）的连续部分在中间态中得以保留，而其余部分则完全展开且无结构。这些部分彼此独立解链。
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