Interactions of tryptophan, tryptophan peptides, and tryptophan alkyl esters at curved membrane interfaces
about
Anisotropic solvent model of the lipid bilayer. 2. Energetics of insertion of small molecules, peptides, and proteins in membranesStructural Basis for the Association of the Redox-sensitive Target of Rapamycin FATC Domain with Membrane-mimetic MicellesStructural adaptations of proteins to different biological membranes.Membrane protein structure determination using crystallography and lipidic mesophases: recent advances and successes.A comprehensive review of the lipid cubic phase or in meso method for crystallizing membrane and soluble proteins and complexes.LCP-Tm: an assay to measure and understand stability of membrane proteins in a membrane environment.Lyotropic liquid crystal engineering moving beyond binary compositional space - ordered nanostructured amphiphile self-assembly materials by design.NMR- and circular dichroism-monitored lipid binding studies suggest a general role for the FATC domain as membrane anchor of phosphatidylinositol 3-kinase-related kinases (PIKK)Crystallizing membrane proteins for structure-function studies using lipidic mesophases.Monoolein: a magic lipid?Life at the border: adaptation of proteins to anisotropic membrane environment.Characterization of residue-dependent differences in the peripheral membrane association of the FATC domain of the kinase 'target of rapamycin' by NMR and CD spectroscopy.Peptide adsorption to lipid bilayers: slow processes revealed by linear dichroism spectroscopy.Tryptophan residues promote membrane association for a plant lipid glycosyltransferase involved in phosphate stress.Effects of different osmolytes on the induced folding of the N-terminal activation domain (AF1) of the glucocorticoid receptor.Conformational properties, membrane interaction, and antibacterial activity of the peptaibiotic chalciporin A: Multitechnique spectroscopic and biophysical investigations on the natural compound and labeled analogs.Target of rapamycin FATC domain as a general membrane anchor: The FKBP-12 like domain of FKBP38 as a case study.
P2860
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P2860
Interactions of tryptophan, tryptophan peptides, and tryptophan alkyl esters at curved membrane interfaces
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
Interactions of tryptophan, tr ...... at curved membrane interfaces
@en
type
label
Interactions of tryptophan, tr ...... at curved membrane interfaces
@en
prefLabel
Interactions of tryptophan, tr ...... at curved membrane interfaces
@en
P2860
P356
P1433
P1476
Interactions of tryptophan, tr ...... at curved membrane interfaces
@en
P2093
Martin Caffrey
P2860
P304
11713-11726
P356
10.1021/BI0608414
P407
P577
2006-10-01T00:00:00Z