Folding of the villin headpiece subdomain from random structures. Analysis of the charge distribution as a function of pH
DR Ripoll, JA Vila, HA Scheraga - Journal of molecular biology, 2004 - Elsevier
The structure of the 36 residue villin headpiece subdomain is investigated with the
electrostatically driven Monte Carlo method. The ECEPP/3 (Empirical Conformational …
electrostatically driven Monte Carlo method. The ECEPP/3 (Empirical Conformational …
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 …
The role of aromatic residues in the hydrophobic core of the villin headpiece subdomain
BS Frank, D Vardar, DA Buckley… - Protein Science, 2002 - Wiley Online Library
Small autonomously folding proteins are of interest as model systems to study protein
folding, as the same molecule can be used for both experimental and computational …
folding, as the same molecule can be used for both experimental and computational …
Probing the folding transition state structure of the villin headpiece subdomain via side chain and backbone mutagenesis
MR Bunagan, J Gao, JW Kelly… - Journal of the American …, 2009 - ACS Publications
Backbone− backbone hydrogen bonds are a common feature of native protein structures,
yet their thermodynamic and kinetic influence on folding has long been debated. This is …
yet their thermodynamic and kinetic influence on folding has long been debated. This is …
Reconciling the solution and X-ray structures of the villin headpiece helical subdomain: molecular dynamics simulations and double mutant cycles reveal a stabilizing …
L Wickstrom, Y Bi, V Hornak, DP Raleigh… - Biochemistry, 2007 - ACS Publications
The 36-residue helical subdomain of the villin headpiece, HP36, is one of the smallest
cooperatively folded proteins, folding on the microsecond time scale. The domain is an …
cooperatively folded proteins, folding on the microsecond time scale. The domain is an …
Peptide models provide evidence for significant structure in the denatured state of a rapidly folding protein: the villin headpiece subdomain
Y Tang, DJ Rigotti, R Fairman, DP Raleigh - Biochemistry, 2004 - ACS Publications
The villin headpiece subdomain is a cooperatively folded 36-residue, three-α-helix protein.
The domain is one of the smallest naturally occurring sequences which has been shown to …
The domain is one of the smallest naturally occurring sequences which has been shown to …
Use of MM‐PB/SA in estimating the free energies of proteins: application to native, intermediates, and unfolded villin headpiece
MR Lee, Y Duan, PA Kollman - Proteins: Structure, Function …, 2000 - Wiley Online Library
We investigated the stability of three different ensembles of the 36‐mer villin headpiece
subdomain, the native, a compact folding intermediate, and the random coil. Structures were …
subdomain, the native, a compact folding intermediate, and the random coil. Structures were …
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 …
Large-scale context in protein folding: villin headpiece
The villin headpiece folds autonomously in vitro forming three α-helical regions. Local
propensities, however, strongly disfavor the formation of the C-terminal helix because most …
propensities, however, strongly disfavor the formation of the C-terminal helix because most …
The unfolded state of the villin headpiece helical subdomain: computational studies of the role of locally stabilized structure
The 36 residue villin headpiece helical subdomain (HP36) is one of the fastest cooperatively
folding proteins, folding on the microsecond timescale. HP36's simple three helix topology …
folding proteins, folding on the microsecond timescale. HP36's simple three helix topology …