Residual structure in a peptide fragment of the outer membrane protein X under denaturing conditions: a molecular dynamics study.
Kräutler
Vincent
V
Laboratory of Physical Chemistry, ETH Zürich, Zürich, Switzerland.
Hiller
Sebastian
S
Hünenberger
Philippe H
PH
D001224:Aspartic Acid / Q000737:chemistry; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D006867:Hydrolases / Q000737:chemistry*; D057927:Hydrophobic and Hydrophilic Interactions; D009682:Magnetic Resonance Spectroscopy; D056004:Molecular Dynamics Simulation; D010446:Peptide Fragments / Q000737:chemistry*; D011489:Protein Denaturation / Q000187:drug effects; D017433:Protein Structure, Secondary / Q000187:drug effects; D012694:Serine / Q000737:chemistry; D013997:Time Factors; D014364:Tryptophan / Q000737:chemistry; D014443:Tyrosine / Q000737:chemistry; D014508:Urea / Q000494:pharmacology*
D001425:Bacterial Outer Membrane Proteins; D029968:Escherichia coli Proteins; D010446:Peptide Fragments; C482905:OmpX protein, E coli; D001224:Aspartic Acid; D014443:Tyrosine; D012694:Serine; D014364:Tryptophan; D014508:Urea; D006867:Hydrolases