Investigating structural changes in the lipid bilayer upon insertion of the transmembrane domain of the membrane-bound protein phospholamban utilizing 31P and 2H solid-state NMR spectroscopy

Investigating structural changes in the lipid bilayer upon insertion of the transmembrane domain of the membrane-bound protein phospholamban utilizing 31P and 2H solid-state NMR spectroscopy

Item
http://www.wikidata.org/entity/Q34185000
Membrane binding of an acyl-lactoferricin B antimicrobial peptide from solid-state NMR experiments and molecular dynamics simulations.Insights on the interactions of synthetic amphipathic peptides with model membranes as revealed by 31P and 2H solid-state NMR and infrared spectroscopiesSpectroscopic validation of the pentameric structure of phospholambanInvestigating the interaction of saposin C with POPS and POPC phospholipids: a solid-state NMR spectroscopic study.CRAC motif peptide of the HIV-1 gp41 protein thins SOPC membranes and interacts with cholesterol.Investigating the interaction between peptides of the amphipathic helix of Hcf106 and the phospholipid bilayer by solid-state NMR spectroscopy.Dynamic conformational responses of a human cannabinoid receptor-1 helix domain to its membrane environment.Probing the interaction of the potassium channel modulating KCNE1 in lipid bilayers via solid-state NMR spectroscopy.Probing the interaction of polyphenols with lipid bilayers by solid-state NMR spectroscopy.Role of the Lipid Environment in the Dimerization of Transmembrane Domains of Glycophorin A.Determining the mode of action involved in the antimicrobial activity of synthetic peptides: a solid-state NMR and FTIR study.Probing the interaction of Arg9Cys mutated phospholamban with phospholipid bilayers by solid-state NMR spectroscopy.Phospholamban and its phosphorylated form interact differently with lipid bilayers: a 31P, 2H, and 13C solid-state NMR spectroscopic study.Transmembrane peptides from tyrosine kinase receptor. Mutation-related behavior in a lipid bilayer investigated by molecular dynamics simulations.Quantifying Binding of Ethylene Oxide-Propylene Oxide Block Copolymers with Lipid Bilayers.Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.
P2860

Investigating structural changes in the lipid bilayer upon insertion of the transmembrane domain of the membrane-bound protein phospholamban utilizing 31P and 2H solid-state NMR spectroscopy

Item
http://www.wikidata.org/entity/Q34185000
description
2004 nî lūn-bûn
@nan
2004 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի մարտին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Investigating structural chang ...... H solid-state NMR spectroscopy
@ast
Investigating structural chang ...... H solid-state NMR spectroscopy
@en
Investigating structural chang ...... H solid-state NMR spectroscopy
@nl
type
label
Investigating structural chang ...... H solid-state NMR spectroscopy
@ast
Investigating structural chang ...... H solid-state NMR spectroscopy
@en
Investigating structural chang ...... H solid-state NMR spectroscopy
@nl
prefLabel
Investigating structural chang ...... H solid-state NMR spectroscopy
@ast
Investigating structural chang ...... H solid-state NMR spectroscopy
@en
Investigating structural chang ...... H solid-state NMR spectroscopy
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P698
P921
P932
P356
P1433
P1476
Investigating structural chang ...... H solid-state NMR spectroscopy
@en
P2093
P2860
P304
P31
P356
10.1016/S0006-3495(04)74224-1
P407
P433
P478
P577
P698
P921
P932