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Steric interactions of valines 1, 5, and 7 in [valine 5, D-alanine 8] gramicidin A channels.Single tryptophan and tyrosine comparisons in the N-terminal and C-terminal interface regions of transmembrane GWALP peptidesComparisons of interfacial Phe, Tyr, and Trp residues as determinants of orientation and dynamics for GWALP transmembrane peptides.Ionization Properties of Histidine Residues in the Lipid Bilayer Membrane Environment.Juxta-terminal Helix Unwinding as a Stabilizing Factor to Modulate the Dynamics of Transmembrane Helices.Conformation of the acylation site of palmitoylgramicidin in lipid bilayers of dimyristoylphosphatidylcholine.Polar groups in membrane channels: consequences of replacing alanines with serines in membrane-spanning gramicidin channels.Properties of membrane-incorporated WALP peptides that are anchored on only one end.Orientation and motion of tryptophan interfacial anchors in membrane-spanning peptides.Tyrosine replacing tryptophan as an anchor in GWALP peptides.Proline kink angle distributions for GWALP23 in lipid bilayers of different thicknesses.Influence of proline upon the folding and geometry of the WALP19 transmembrane peptide.Sensitivity of single membrane-spanning alpha-helical peptides to hydrophobic mismatch with a lipid bilayer: effects on backbone structure, orientation, and extent of membrane incorporation.Interfacial anchor properties of tryptophan residues in transmembrane peptides can dominate over hydrophobic matching effects in peptide-lipid interactions.Amino acid sequence modulation of gramicidin channel function: effects of tryptophan-to-phenylalanine substitutions on the single-channel conductance and duration.Lipid interactions of acylated tryptophan-methylated lactoferricin peptides by solid-state NMR.Influence of lipid/peptide hydrophobic mismatch on the thickness of diacylphosphatidylcholine bilayers. A 2H NMR and ESR study using designed transmembrane alpha-helical peptides and gramicidin A.Heptapeptide mimic of ohmefentanyl binding in the discontinuous mu-opiod receptor.CorrectionsThe Effects of Hydrophobic Mismatch between Phosphatidylcholine Bilayers and Transmembrane α-Helical Peptides Depend on the Nature of Interfacially Exposed Aromatic and Charged Residues†Neighboring Aliphatic/Aromatic Side Chain Interactions between Residues 9 and 10 in Gramicidin Channels†Tryptophan-Anchored Transmembrane Peptides Promote Formation of Nonlamellar Phases in Phosphatidylethanolamine Model Membranes in a Mismatch-Dependent Manner†Modulation of Gramicidin Channel Structure and Function by the Aliphatic “Spacer” Residues 10, 12, and 14 between the Tryptophans†Palmitoylation-Induced Conformational Changes of Specific Side Chains in the Gramicidin Transmembrane ChannelA general method for the preparation of mixed micelles of hydrophobic peptides and sodium dodecyl sulphateTransmembrane Helix Integrity versus Fraying To Expose Hydrogen Bonds at a Membrane-Water InterfaceInfluence of Lipid Saturation, Hydrophobic Length and Cholesterol on Double-Arginine-Containing Helical Peptides in Bilayer MembranesBreaking the Backbone: Central Arginine Residues Induce Membrane Exit and Helix Distortions within a Dynamic Membrane Peptide
P50
Q30582332-194590D8-1481-4277-A664-94CFA12A49C8Q30674488-601D5851-52B1-423B-AF71-FED6032F259BQ30820815-F5BAAA2C-6416-47B3-A8F5-01571E014C09Q31116183-A0F03359-A550-46AA-A3BB-196119E792DAQ36763187-C77CF578-7719-4BB3-8E60-69A88CD858FBQ36800010-B49DDADF-FE1E-423A-B08A-A72756F9E762Q42114878-0F9604E5-F9E6-418E-A53C-47D6A3611E28Q42423415-F12FFCE2-352A-4E62-85DB-88DE67870AC6Q42434329-9C0F3AC1-31BD-404F-9AF9-384BE7AE2677Q42566295-FE7518EE-870E-49A2-901F-789C10295169Q43066374-173D9128-21FA-4B80-B9C9-8AC6F5EF8226Q43248074-C2DA912F-3545-41FB-A06F-57F6010F3EF7Q43577465-628E42D2-083F-4032-A5F3-78BF0199DC3EQ44430419-E4CCD417-D1DF-408B-A2D5-42CC01E601B9Q44512850-F9EB8DEF-8F49-48CA-B554-9682E0CDD3C1Q46559492-BD33E836-0D47-4D6F-93A9-B6170C24C7C0Q47901015-F347742C-E9FB-4B53-AB34-9FEF52C33309Q51220140-EA9909A4-B4D2-4267-9A3D-B84130E38FD3Q57955980-ADF8A387-C779-4C8A-97AA-93590D32E142Q57956003-B96CE3B6-AD50-4199-A9E6-19E8A1EFB09AQ57956007-6D20BCCB-9F35-453A-8A4A-38A8DDC847DBQ57956011-C9D40380-8816-4219-AC0E-3DD5B1C76F66Q57956013-38B8947C-FCFA-4353-9E9E-75B4A930FB0EQ57956019-40D3E6E4-6FAC-4B43-AA95-73BCB41E27CFQ57956022-631AB57E-7A76-4F79-8E81-6C349479797EQ90629248-616589C5-E67A-47B9-9F2F-E9E58B484404Q92438597-872A3BA2-8F04-4245-9FC7-8E267D8062D2Q93098501-EC1EC9BC-3ABA-46F3-89DF-BDDC77C75AE9
P50
description
hulumtuese
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Denise V Greathouse
@ast
Denise V Greathouse
@en
Denise V Greathouse
@es
Denise V Greathouse
@nl
Denise V Greathouse
@sl
type
label
Denise V Greathouse
@ast
Denise V Greathouse
@en
Denise V Greathouse
@es
Denise V Greathouse
@nl
Denise V Greathouse
@sl
prefLabel
Denise V Greathouse
@ast
Denise V Greathouse
@en
Denise V Greathouse
@es
Denise V Greathouse
@nl
Denise V Greathouse
@sl
P106
P21
P31
P496
0000-0001-7104-8499
P569
2000-01-01T00:00:00Z