NMR structure of the 35-residue villin headpiece subdomain
Copyright policy )NMR structure of the 35-residue villin headpiece subdomain
The NMR structure of an autonomously folding subdomain from villin headpiece is reported. It forms a novel three helix structure with the actin-binding residues arrayed on the C-terminal helix.
- Boston College United States
- Howard Hughes Medical Institute United States
- Massachusetts Institute of Technology United States
- Boston University United States
Models, Molecular, Magnetic Resonance Spectroscopy, Protein Conformation, Calcium-Binding Proteins, Microfilament Proteins, Molecular Sequence Data, Hydrogen Bonding, Peptide Fragments, Protein Structure, Secondary, Models, Structural, Amino Acid Sequence, Carrier Proteins, Software
Models, Molecular, Magnetic Resonance Spectroscopy, Protein Conformation, Calcium-Binding Proteins, Microfilament Proteins, Molecular Sequence Data, Hydrogen Bonding, Peptide Fragments, Protein Structure, Secondary, Models, Structural, Amino Acid Sequence, Carrier Proteins, Software
citations This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).310 popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.Top 1% influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).Top 1% impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.Top 10%
Citations provided by BIP!Popularity provided by BIP!