Effect of modulating unfolded state structure on the folding kinetics of the villin headpiece subdomain
SH Brewer, DM Vu, Y Tang, Y Li… - Proceedings of the …, 2005 - National Acad Sciences
Equilibrium Fourier transform infrared (FTIR) and temperature-jump (T-jump) IR
spectroscopic techniques were used to study the thermodynamics and kinetics of the …
spectroscopic techniques were used to study the thermodynamics and kinetics of the …
Native like structure in the unfolded state of the villin headpiece helical subdomain, an ultrafast folding protein
W Meng, B Shan, Y Tang, DP Raleigh - Protein Science, 2009 - Wiley Online Library
The villin headpiece subdomain, HP36, is the smallest naturally occurring protein that folds
cooperatively. Its small size, rapid folding, and simple three‐helix topology have made it an …
cooperatively. Its small size, rapid folding, and simple three‐helix topology have made it an …
High-resolution x-ray crystal structures of the villin headpiece subdomain, an ultrafast folding protein
TK Chiu, J Kubelka, R Herbst-Irmer… - Proceedings of the …, 2005 - National Acad Sciences
The 35-residue subdomain of the villin headpiece (HP35) is a small ultrafast folding protein
that is being intensely studied by experiments, theory, and simulations. We have solved the …
that is being intensely studied by experiments, theory, and simulations. We have solved the …
Molecular mechanism behind the fast folding/unfolding transitions of villin headpiece subdomain: Hierarchy and heterogeneity
T Mori, S Saito - The Journal of Physical Chemistry B, 2016 - ACS Publications
Proteins involve motions over a wide range of spatial and temporal scales. While the large
conformational changes, such as folding and functioning, are slow and appear to occur in a …
conformational changes, such as folding and functioning, are slow and appear to occur in a …
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 early stage of folding of villin headpiece subdomain observed in a 200-nanosecond fully solvated molecular dynamics simulation
Y Duan, L Wang, PA Kollman - Proceedings of the National …, 1998 - National Acad Sciences
A new approach in implementing classical molecular dynamics simulation for parallel
computers has enabled a simulation to be carried out on a protein with explicit …
computers has enabled a simulation to be carried out on a protein with explicit …
Characterizing a partially folded intermediate of the villin headpiece domain under non-denaturing conditions: contribution of His41 to the pH-dependent stability of …
MJ Grey, Y Tang, E Alexov, CJ McKnight… - Journal of molecular …, 2006 - Elsevier
The contribution of interactions involving the imidazole ring of His41 to the pH-dependent
stability of the villin headpiece (HP67) N-terminal subdomain has been investigated by …
stability of the villin headpiece (HP67) N-terminal subdomain has been investigated by …
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 …
Heterogeneity in the folding of villin headpiece subdomain HP36
S Nagarajan, S Xiao, DP Raleigh… - The Journal of Physical …, 2018 - ACS Publications
Small single domain proteins that fold on the microsecond time scale have been the subject
of intense interest as models for probing the complexity of folding energy landscapes. The …
of intense interest as models for probing the complexity of folding energy landscapes. The …
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 …