Bioactive Conformation II
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...
Guardado en:
| Autor principal: | |
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| Formato: | Livre numérique |
| Lenguaje: | Anglais |
| Publicado: |
Berlin, Heidelberg :
Springer Berlin Heidelberg
[20..].
Cham : Springer Nature |
| Edición: | 1st ed. 2008. |
| Colección: | Topics in Current Chemistry
273 |
| Materias: | |
| Acceso en línea: | Accès sur la plateforme de l'éditeur Accès sur la plateforme Istex Accès Université d'Orléans Accès INSA CVL |
| Nota: |
Archives Springer e-books (Licence nationale) Archives Springer e-books (Licence nationale) |
| Autres localisations: | Voir dans le Sudoc |
| Edition sous un autre format: | • Bioactive conformation, II, volume editor : Thomas Peters, Berlin, Springer, 2008, 1 vol. (XII-233 p.), Topics in current chemistry, 978-3-540-49079-1 |
| Sumario: | 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, totransferred dipolar couplings,toSTD (saturation transfer difference) NMR techniques. Incaseswhere tightbinding inthesub-nanomolar rangeprevents the analysis of the bioactive conformation via free ligand signals, the ligand proteincomplexhas tobeanalyzed withproteinNMR-based techniques orby crystallography.Sincethisareahasbeenthesubjectofmanyreviewsandmo- graphsitwill not be covered here in particular detail. As a unifying theme, all contributionstargetthequestionofhowmolecular recognitionofbiologically active molecules is achieved on the atomic scale. Depending on the research topic the results from these studies have a strong impact not only in basic research but also in several ?elds of application ranging frompharmaceutical applications tothe use of biomolecules as, for example, cryoprotectants |
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| Notas: | Archives Springer e-books (Licence nationale) Archives Springer e-books (Licence nationale) |
| ISBN: | 9783540490807 |
| ISSN: | 1436-5049 |
| Acceso: | Accès en ligne pour les établissements français bénéficiaires des licences nationales Accès soumis à abonnement pour tout autre établissement Conditions particulières de réutilisation pour les bénéficiaires des licences nationales. https://www.licencesnationales.fr/springer-nature-ebooks-contrat-licence-ln-2017 |