Titre de série :	Topics in Current Chemistry
Titre :	Vol.273 : Bioactive conformation II
Type de document :	texte imprimé
Auteurs :	Thomas Peters, Éditeur scientifique
Editeur :	Berlin, Heidelberg : Springer
Année de publication :	2007
Collection :	Topics in Current Chemistry, ISSN 0340-1022 num. 273
Importance :	xii, 233 p.
Format :	24 cm
ISBN/ISSN/EAN :	978-3-540-49079-1
Langues :	Anglais (eng)
Note de contenu :	"* NMR-based strategies to elucidate bioactive conformations of weakly binding ligands * Quantitative analysis of STD-NMR spectra of reversibly forming ligand–receptor complexes * Structural and functional studies of peptide–carbohydrate mimicry * Studies on the conformational features of neomycin-b and its molecular recognition by RNA and bacterial defense proteins * Solid state NMR structure analysis of the antimicrobial peptide gramicidin S in lipid membranes: Concentration-dependent re-alignment and self-assembly as a ?-barrel * Modulation of the bioactive conformation of transforming growth factor ?: Possible implications of cation binding for biological function * Molecular recognition of ligands by native viruses and virus-like particles as studied by NMR experiments * Investigation of proteins in living bacteria with in-cell NMR experiments."
Cote :	EXCLU (SdL)
Num_Inv :	2847

Topics in Current Chemistry. Vol.273 : Bioactive conformation II [texte imprimé] / Thomas Peters, Éditeur scientifique . - Berlin, Heidelberg : Springer, 2007 . - xii, 233 p. ; 24 cm. - (Topics in Current Chemistry, ISSN 0340-1022; 273) .
ISBN : 978-3-540-49079-1
Langues : Anglais (eng)

Note de contenu :	"* NMR-based strategies to elucidate bioactive conformations of weakly binding ligands * Quantitative analysis of STD-NMR spectra of reversibly forming ligand–receptor complexes * Structural and functional studies of peptide–carbohydrate mimicry * Studies on the conformational features of neomycin-b and its molecular recognition by RNA and bacterial defense proteins * Solid state NMR structure analysis of the antimicrobial peptide gramicidin S in lipid membranes: Concentration-dependent re-alignment and self-assembly as a ?-barrel * Modulation of the bioactive conformation of transforming growth factor ?: Possible implications of cation binding for biological function * Molecular recognition of ligands by native viruses and virus-like particles as studied by NMR experiments * Investigation of proteins in living bacteria with in-cell NMR experiments."
Cote :	EXCLU (SdL)
Num_Inv :	2847