通过不同温度下的分子动力学模拟研究BBA1的稳定性和展开机制。
Study of the stability and unfolding mechanism of BBA1 by molecular dynamics simulations at different temperatures.
作者信息
Wang L, Duan Y, Shortle R, Imperiali B, Kollman P A
机构信息
Department of Pharmaceutical Chemistry, University of California, San Francisco 94143-0446, USA.
出版信息
Protein Sci. 1999 Jun;8(6):1292-304. doi: 10.1110/ps.8.6.1292.
BBA1 is a designed protein that has only 23 residues. It is the smallest protein without disulfide bridges that has a well-defined tertiary structure in solution. We have performed unfolding molecular dynamics simulations on BBA1 and some of its mutants at 300, 330, 360, and 400 K to study their kinetic stability as well as the unfolding mechanism of BBA1. It was shown that the unfolding simulations can provide insights into the forces that stabilize the protein. Packing, hydrophobic interactions, and a salt bridge between Asp12 and Lys16 were found to be important to the protein's stability. The unfolding of BBA1 goes through two major steps: (1) disruption of the hydrophobic core and (2) unfolding of the helix. The beta-hairpin remains stable in the unfolding because of the high stability of the type II' turn connecting the two beta-strands.
BBA1是一种仅含23个残基的设计蛋白。它是在溶液中具有明确三级结构的最小的无二硫键蛋白。我们对BBA1及其一些突变体在300、330、360和400 K下进行了去折叠分子动力学模拟，以研究它们的动力学稳定性以及BBA1的去折叠机制。结果表明，去折叠模拟可以深入了解稳定蛋白质的作用力。堆积作用、疏水相互作用以及Asp12和Lys16之间的盐桥被发现对蛋白质的稳定性很重要。BBA1的去折叠经历两个主要步骤：（1）疏水核心的破坏和（2）螺旋的去折叠。由于连接两条β链的II'型转角具有高稳定性，β发夹在去折叠过程中保持稳定。
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