Optimized folding simulations of protein A
Document Type
Article
Publication Date
11-1-2007
Abstract
We describe optimized parallel tempering simulations of the 46-residue B-fragment of protein A. Native-like configurations with a root-mean-square deviation of ≈ 3 Å to the experimentally determined structure (Protein Data Bank identifier 1BDD) are found. However, at biologically relevant temperatures such conformations appear with only ≈ 10 % frequency in our simulations. Possible shortcomings in our energy function are discussed. © 2007 EDP Sciences, Società Italiana di Fisica and Springer-Verlag.
Publication Title
European Physical Journal E
Recommended Citation
Trebst, S.,
&
Hansmann, U.
(2007).
Optimized folding simulations of protein A.
European Physical Journal E,
24(3), 311-316.
http://doi.org/10.1140/epje/i2007-10241-1
Retrieved from: https://digitalcommons.mtu.edu/michigantech-p/12425