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Chemistry

University of Arkansas, Fayetteville

Theses/Dissertations

Transmembrane peptides

Publication Year

Articles 1 - 2 of 2

Full-Text Articles in Physical Sciences and Mathematics

Influence Of Histidine Residues, Ph And Charge Interactions On Membrane-Spanning Peptides, Ashley N. Henderson May 2017

Influence Of Histidine Residues, Ph And Charge Interactions On Membrane-Spanning Peptides, Ashley N. Henderson

Graduate Theses and Dissertations

Designed transmembrane peptides were employed for investigations of histidine residues within the hydrophobic environment of the lipid bilayer by means of oriented solid-state deuterium NMR spectroscopy. Using the model peptide GWALP23 sequence (GGALW(LA)6LWLAGA) as a host framework, the effects of single and double histidine mutations were explored. Replacement of leucine residue 12 to polar neutral histidine had little influence on the peptide average orientation, however under strongly acidic pH conditions in DOPC bilayers, the histidine becomes positively charged (pKa 2.5) and the GWALP23-H12 peptide exits the membrane and adopts a surface-bound orientation. Conversely, mutation of leucine 14 to neutral histidine …


Protein-Lipid Interactions: Influence Of Anchoring Groups And Buried Arginine On The Properties Of Membrane-Spanning Peptides, Vitaly V. Vostrikov May 2011

Protein-Lipid Interactions: Influence Of Anchoring Groups And Buried Arginine On The Properties Of Membrane-Spanning Peptides, Vitaly V. Vostrikov

Graduate Theses and Dissertations

Designed transmembrane peptides were employed for investigations of protein-lipid interactions by means of oriented solid-state deuterium NMR spectroscopy using isotope-enriched alanine residues. Using the model GWALP23 sequence (GGALW(LA)6LWLAGA) as a host peptide having single interfacial tryptophan anchor residues, the effects of different guest mutations were explored. Replacements of glycine residues 2 and 22 to positively charged lysine or arginine on both termini had little influence on the peptide average orientation. Conversely, glycine to tryptophan substitutions had profound effects, manifested in the increased dynamics and altered tilt direction of the peptide. While the charged residues at the peptide termini did not …