Multistate folding of the villin headpiece domain
Y Tang, MJ Grey, J McKnight, AG Palmer III… - Journal of molecular …, 2006 - Elsevier
The villin headpiece (HP67) is a 67 residue, monomeric protein derived from the C-terminal
domain of villin. Wild-type HP67 (WT HP67) is the smallest fragment of villin that retains …
domain of villin. Wild-type HP67 (WT HP67) is the smallest fragment of villin that retains …
Roadmap methods for protein folding
M Moll, D Schwarz, LE Kavraki - Protein Structure Prediction, 2008 - Springer
Protein folding refers to the process whereby a protein assumes its intricate three-
dimensional shape. This chapter reviews a class of methods for studying the folding process …
dimensional shape. This chapter reviews a class of methods for studying the folding process …
Study of the Villin headpiece folding dynamics by combining coarse‐grained Monte Carlo evolution and all‐atom molecular dynamics
GMS De Mori, G Colombo… - … : Structure, Function, and …, 2005 - Wiley Online Library
The folding mechanism of the Villin headpiece (HP36) is studied by means of a novel
approach which entails an initial coarse‐grained Monte Carlo (MC) scheme followed by all …
approach which entails an initial coarse‐grained Monte Carlo (MC) scheme followed by all …
Improvement of the treatment of loop structures in the UNRES force field by inclusion of coupling between backbone-and side-chain-local conformational states
The UNited RESidue (UNRES) coarse-grained model of polypeptide chains, developed in
our laboratory, enables us to carry out millisecond-scale molecular-dynamics simulations of …
our laboratory, enables us to carry out millisecond-scale molecular-dynamics simulations of …
Response of villin headpiece-capped gold nanoparticles to ultrafast laser heating
The integrity of a small model protein, the 36-residue villin headpiece HP36, attached to
gold nanoparticles (AuNP) is examined, and its response to laser excitation of the AuNPs is …
gold nanoparticles (AuNP) is examined, and its response to laser excitation of the AuNPs is …
Predicting the effect of a point mutation on a protein fold: the villin and advillin headpieces and their Pro62Ala mutants
Homology modeling of unknown proteins is based on the assumption that highly similar
sequences are likely to share the same fold. However, this does not provide any information …
sequences are likely to share the same fold. However, this does not provide any information …
Phylogeny of protein-folding trajectories reveals a unique pathway to native structure
M Ota, M Ikeguchi, A Kidera - Proceedings of the National …, 2004 - National Acad Sciences
To scrutinize how a protein folds at atomic resolution, we performed 200 molecular
dynamics simulations (each of 50 ns) of the miniprotein Trp-cage on the computational grid …
dynamics simulations (each of 50 ns) of the miniprotein Trp-cage on the computational grid …
Analysis of core packing in a cooperatively folded miniature protein: the ultrafast folding villin headpiece helical subdomain
S Xiao, Y Bi, B Shan, DP Raleigh - Biochemistry, 2009 - ACS Publications
The helical subdomain of the villin headpiece is the smallest naturally occurring
cooperatively folded protein. Its small size, simple three-helix topology, and very rapid …
cooperatively folded protein. Its small size, simple three-helix topology, and very rapid …
Determination of side‐chain‐rotamer and side‐chain and backbone virtual‐bond‐stretching potentials of mean force from AM1 energy surfaces of terminally‐blocked …
U Kozłowska, GG Maisuradze, A Liwo… - Journal of …, 2010 - Wiley Online Library
Using the harmonic‐approximation approach of the accompanying article and AM1 energy
surfaces of terminally blocked amino‐acid residues, we determined physics‐based side …
surfaces of terminally blocked amino‐acid residues, we determined physics‐based side …
NMR characterization of a peptide model provides evidence for significant structure in the unfolded state of the villin headpiece helical subdomain
Y Tang, MJ Goger, DP Raleigh - Biochemistry, 2006 - ACS Publications
The villin headpiece subdomain (HP36) is the smallest naturally occurring protein that folds
cooperatively. The protein folds on a microsecond time scale. Its small size and very rapid …
cooperatively. The protein folds on a microsecond time scale. Its small size and very rapid …