Department of Chemistry and Chemical Biology, Baker Laboratory, Cornell University, Ithaca, New York, USA.
Department of Biochemistry and Biophysics, University of Rochester School of Medicine and Dentistry, Rochester, New York, USA.
Biopolymers. 2021 Oct;112(10):e23411. doi: 10.1002/bip.23411. Epub 2020 Dec 3.
Using bioinformatic methods for treating protein dynamics, developed in earlier work, we study the relationship between sequence mobility and dynamics in proteins. It is shown that sequence mobility drives a transition between two dynamic regimes in proteins, and that the specific details of this transition differ qualitatively between α-helical proteins and those in other structural classes. We examine the possibility that conformational switching is related to dynamic switching, by considering a specific system of sequences which exhibit the switching phenomenon. It is shown that a relationship between dynamic and conformational switching is entirely plausible.
运用在早期工作中开发的处理蛋白质动力学的生物信息学方法，我们研究了序列可动性与蛋白质动力学之间的关系。结果表明，序列可动性驱动蛋白质中两种动力学状态之间的转变，并且这种转变的具体细节在α-螺旋蛋白和其他结构类别之间存在定性差异。通过考虑表现出这种转变现象的特定序列系统，我们研究了构象转变与动力学转变之间存在关系的可能性。结果表明，动力学和构象转变之间存在关系是完全合理的。
