article · Proteins Structure Function and Bioinformatics · 2003

Parallel tempering simulations of HP‐36

Chai‐Yu Lin, Chin‐Kun Hu, Ulrich H. E. Hansmann

Cited by 94Abstract and details only

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.

Cite this paper

APA 7

Lin, C., Hu, C., & Hansmann, U. H. E. (2003). Parallel tempering simulations of HP‐36. Proteins Structure Function and Bioinformatics, 52(3), 436–445. https://doi.org/10.1002/prot.10351

MLA 9

Lin, Chai‐Yu, et al. “Parallel tempering simulations of HP‐36.” Proteins Structure Function and Bioinformatics, vol. 52, no. 3, 2003, pp. 436–45, https://doi.org/10.1002/prot.10351.

Chicago

Lin, Chai‐Yu, Chin‐Kun Hu, and Ulrich H. E. Hansmann. 2003. “Parallel tempering simulations of HP‐36.” Proteins Structure Function and Bioinformatics 52 (3): 436–45. https://doi.org/10.1002/prot.10351.

Harvard

Lin, C., Hu, C. and Hansmann, U.H.E. (2003) ‘Parallel tempering simulations of HP‐36’, Proteins Structure Function and Bioinformatics, 52(3), pp. 436–445. Available at: https://doi.org/10.1002/prot.10351.

BibTeX

@article{lin2003parallel,
  title = {{Parallel tempering simulations of HP‐36}},
  author = {Lin, Chai‐Yu and Hu, Chin‐Kun and Hansmann, Ulrich H. E.},
  journal = {Proteins Structure Function and Bioinformatics},
  volume = {52},
  number = {3},
  pages = {436--445},
  year = {2003},
  doi = {10.1002/prot.10351}
}

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