Parallel tempering simulations of HP-36

Authors

Chai Yu Lin, Academia Sinica, Institute Of Physics
Chin Kun Hu, Academia Sinica, Institute Of Physics
Ulrich H.E Hansmann, Michigan Technological UniversityFollow

Document Type

Article

Publication Date

8-15-2003

Department

Department of Physics

Abstract

We report results from all-atom Monte Carlo simulations of the 36-residue villin headpiece subdomain HP-36. Protein-solvent interactions are approximated by an implicit solvent model. The parallel tempering is used to overcome the problem of slow convergence in low-temperature protein simulations. Our results show that this technique allows one to sample native-like structures of small proteins and points out the need for improved energy functions.

Publisher's Statement

© 2003 Wiley-Liss, Inc. Publisher’s version of record: https://doi.org/10.1002/prot.10351

Publication Title

Proteins: Structure, Function and Genetics

Recommended Citation

Lin, C., Hu, C., & Hansmann, U. H. (2003). Parallel tempering simulations of HP-36. Proteins: Structure, Function and Genetics, 52(3), 436-445. http://doi.org/10.1002/prot.10351
Retrieved from: https://digitalcommons.mtu.edu/michigantech-p/3857