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Bioactive Conformation I
Speci?c binding of a ligand to a receptor is a key step in a variety of biol- ical processes, such as immune reactions, enzyme cascades, or intracellular transport processes. The ligand receptor terminology implies that the rec- tor molecule is signi?cantly larger than the ligand, and the term bioac...
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| Auteur principal : | |
|---|---|
| Format : | Livre |
| Langue : | anglais |
| Titre complet : | Bioactive Conformation I / edited by Thomas Peters. |
| Édition : | 1st ed. 2007. |
| Publié : |
Berlin, Heidelberg :
Springer Berlin Heidelberg
, [20..] Cham : Springer Nature |
| Collection : | Topics in current chemistry (Internet) ; 272 |
| Accès en ligne : |
Accès Nantes Université
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| Condition d'utilisation et de reproduction : | Conditions particulières de réutilisation pour les bénéficiaires des licences nationales : https://www.licencesnationales.fr/springer-nature-ebooks-contrat-licence-ln-2017 |
| Contenu : | Spatial Screening for the Identification of the Bioactive Conformation of Integrin Ligands. Dynamics and Thermodynamics of Ligand Protein Interactions. The Fibroblast Growth Factor (FGF) FGF Receptor Complex: Progress Towards the Physiological State. Characterization of Interactions Between Misfolding Proteins and Molecular Chaperones by NMR Spectroscopy. NMR Analysis of Bioprotective Sugars: Sucrose and Oligomeric (1?2)-?-D-glucopyranosyl-(1?2)-?-D-fructofuranosides. Residual Dipolar Couplings Report on the Active Conformation of Rhodopsin-Bound Protein Fragments. Glycosyltransferase Structure and Function. Exploiting Ligand and Receptor Adaptability in Rational Drug Design Using Dynamics and Structure-Based Strategies |
| Sujets : | |
| Documents associés : | Autre format:
Bioactive conformation |
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| 200 | 1 | |a Bioactive Conformation I |f edited by Thomas Peters. | |
| 205 | |a 1st ed. 2007. | ||
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| 225 | 0 | |a Topics in Current Chemistry |x 1436-5049 |v 272 | |
| 327 | 1 | |a Spatial Screening for the Identification of the Bioactive Conformation of Integrin Ligands |a Dynamics and Thermodynamics of Ligand Protein Interactions |a The Fibroblast Growth Factor (FGF) FGF Receptor Complex: Progress Towards the Physiological State |a Characterization of Interactions Between Misfolding Proteins and Molecular Chaperones by NMR Spectroscopy |a NMR Analysis of Bioprotective Sugars: Sucrose and Oligomeric (1?2)-?-D-glucopyranosyl-(1?2)-?-D-fructofuranosides |a Residual Dipolar Couplings Report on the Active Conformation of Rhodopsin-Bound Protein Fragments |a Glycosyltransferase Structure and Function |a Exploiting Ligand and Receptor Adaptability in Rational Drug Design Using Dynamics and Structure-Based Strategies | |
| 330 | |a Speci?c binding of a ligand to a receptor is a key step in a variety of biol- ical processes, such as immune reactions, enzyme cascades, or intracellular transport processes. The ligand receptor terminology implies that the rec- tor molecule is signi?cantly larger than the ligand, and the term bioactive conformation usually characterizes the conformation of a ligand when it is bound to a receptor. In a more general sense, bioactive conformation applies toanymoleculeinabiologicallyrelevantboundstateregardlessofsizecons- erations. Mostofthecontributions tothisbookaddressligandsthat aremuch smaller than their receptors. X-ray crystallography and high resolution NMR spectroscopy are the two main experimental techniques used to study bioactive conformations. The- fore,the twovolumes ofthisbookcover approachesthat use either ofthetwo techniques, or a combination thereof. The combination of X-ray crystallog- phy and NMR spectroscopy is particularly useful when a crystal structure of areceptorprotein,butnotofthereceptorprotein ligandcomplex,isavailable. Anumberofexperimentaltechniquestoanalyzethebioactiveconformationof aligandwithNMRarebasedontheobservationoftheresonancesignalsofthe free ligand that is in exchange with the bound ligand. Several chapters focus onsuchapproachesthat rangefrom classical transferredNOEexperiments, totransferreddipolarcouplings,toSTD(SaturationTransferDifference)NMR techniques. Incaseswhere tightbinding inthesub-nanomolar rangeprevents the analysis of the bioactive conformation via free ligand signals, the ligand protein complex has to be analyzed with protein NMR-based techniques or by crystallography. Since this area has been the subject of many reviews and monographs it will not be covered here in particular detail. As a unifying theme, all contributions target the question of how molecular recognition of biologically active molecules is achieved on the atomic scale | ||
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