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villin headpiece subdomain peptide

Known as: HP 36, HP-36, HP36 peptide 
National Institutes of Health

Papers overview

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2010
2010
We have investigated the folding pathway of the 36‐residue villin headpiece subdomain (HP‐36) by action‐derived molecular… 
Highly Cited
2008
Highly Cited
2008
Water molecules around a protein exhibit slow dynamics with respect to that of pure bulk water. One important issue in protein… 
2008
2008
Atomistic molecular dynamics simulations of the folded native structure and a partially unfolded molten globule structure of the… 
2007
2007
An atomistic molecular dynamics simulation has been carried out to understand the low-frequency intermolecular vibrational… 
2007
2007
We investigate the relation between backbone and side-chain ordering in a small protein. For this purpose, we have performed… 
2007
2007
An atomistic molecular dynamics simulation of the protein villin headpiece subdomain or HP-36 has been carried out with explicit… 
Highly Cited
2005
Highly Cited
2005
The heterogeneous nature of a protein surface plays an essential role in its biological activity and molecular recognition, and… 
Highly Cited
2005
Highly Cited
2005
The structure and dynamics of water around a protein is expected to be sensitive to the details of the adjacent secondary… 
2004
2004
Abstract.Determination of the native state of a protein from its amino acid sequence is the goal of protein folding simulations… 
Highly Cited
2003
Highly Cited
2003
We report results from all‐atom Monte Carlo simulations of the 36‐residue villin headpiece subdomain HP‐36. Protein‐solvent…