Pages that link to "Q43988077"
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The following pages link to Application of REDOR subtraction for filtered MAS observation of labeled backbone carbons of membrane-bound fusion peptides (Q43988077):
Displaying 23 items.
- On the role of NMR spectroscopy for characterization of antimicrobial peptides (Q26830116) (← links)
- Membrane Fusion and Infection of the Influenza Hemagglutinin (Q30396401) (← links)
- Solid-State Nuclear Magnetic Resonance Evidence for Parallel and Antiparallel Strand Arrangements in the Membrane-Associated HIV-1 Fusion Peptide (Q33193682) (← links)
- HIV fusion peptide penetrates, disorders, and softens T-cell membrane mimics. (Q34131438) (← links)
- Oligomeric beta-structure of the membrane-bound HIV-1 fusion peptide formed from soluble monomers (Q34187142) (← links)
- Structure and orientation of pardaxin determined by NMR experiments in model membranes (Q34803793) (← links)
- REDOR solid-state NMR as a probe of the membrane locations of membrane-associated peptides and proteins (Q35210688) (← links)
- Closed and Semiclosed Interhelical Structures in Membrane vs Closed and Open Structures in Detergent for the Influenza Virus Hemagglutinin Fusion Peptide and Correlation of Hydrophobic Surface Area with Fusion Catalysis (Q35782869) (← links)
- Frequency-selective heteronuclear dephasing and selective carbonyl labeling to deconvolute crowded spectra of membrane proteins by magic angle spinning NMR. (Q35894301) (← links)
- Effect of the HIV-1 fusion peptide on the mechanical properties and leaflet coupling of lipid bilayers. (Q36678759) (← links)
- Structure, topology, and tilt of cell-signaling peptides containing nuclear localization sequences in membrane bilayers determined by solid-state NMR and molecular dynamics simulation studies (Q36857817) (← links)
- Quantitation of recombinant protein in whole cells and cell extracts via solid-state NMR spectroscopy (Q37074027) (← links)
- Solid-state NMR spectroscopy of human immunodeficiency virus fusion peptides associated with host-cell-like membranes: 2D correlation spectra and distance measurements support a fully extended conformation and models for specific antiparallel strand (Q41534544) (← links)
- Interaction of alamethicin with ether-linked phospholipid bilayers: oriented circular dichroism, 31P solid-state NMR, and differential scanning calorimetry studies. (Q41961282) (← links)
- Conformational flexibility and strand arrangements of the membrane-associated HIV fusion peptide trimer probed by solid-state NMR spectroscopy (Q41987173) (← links)
- Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel β sheet fusion peptide structure in the final six-helix bundle state (Q42003499) (← links)
- Solid-state nuclear magnetic resonance measurements of HIV fusion peptide to lipid distances reveal the intimate contact of beta strand peptide with membranes and the proximity of the Ala-14-Gly-16 region with lipid headgroups (Q42009823) (← links)
- HIV fusion peptide and its cross-linked oligomers: efficient syntheses, significance of the trimer in fusion activity, correlation of beta strand conformation with membrane cholesterol, and proximity to lipid headgroups (Q42196734) (← links)
- pH-dependent vesicle fusion induced by the ectodomain of the human immunodeficiency virus membrane fusion protein gp41: Two kinetically distinct processes and fully-membrane-associated gp41 with predominant β sheet fusion peptide conformation (Q42202737) (← links)
- Utilizing afterglow magnetization from cross-polarization magic-angle-spinning solid-state NMR spectroscopy to obtain simultaneous heteronuclear multidimensional spectra (Q42274680) (← links)
- Nuclear magnetic resonance evidence for retention of a lamellar membrane phase with curvature in the presence of large quantities of the HIV fusion peptide (Q42929024) (← links)
- Residue-specific membrane location of peptides and proteins using specifically and extensively deuterated lipids and ¹³C-²H rotational-echo double-resonance solid-state NMR. (Q43053935) (← links)
- 13C-13C and (15)N-(13)C correlation spectroscopy of membrane-associated and uniformly labeled human immunodeficiency virus and influenza fusion peptides: amino acid-type assignments and evidence for multiple conformations (Q44018489) (← links)