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dc.contributor.authorLaufer, B.
dc.contributor.authorFrank, A.O.
dc.contributor.authorChatterjee, J.
dc.contributor.authorNeubauer, T.
dc.contributor.authorMas Moruno, Carlos
dc.contributor.authorKummerlöwe, G.
dc.contributor.authorKessler, H.
dc.contributor.otherUniversitat Politècnica de Catalunya. Departament de Ciència dels Materials i Enginyeria Metal·lúrgica
dc.date.accessioned2014-09-18T11:07:17Z
dc.date.created2010
dc.date.issued2010
dc.identifier.citationLaufer, B. [et al.]. The impact of amino acid side chain mutations in conformational design of peptides and proteins. "Chemistry: a european journal", 2010, vol. 16, núm. 18, p. 5385-5390.
dc.identifier.issn0947-6539
dc.identifier.urihttp://hdl.handle.net/2117/24098
dc.description.abstractLocal energetic effects of amino acid replacements are often considered to have only a moderate influence on the backbone conformation of proteins or peptides. As these effects are difficult to determine experimentally, no comparison has yet been performed. However, knowledge of the influence of side chain mutations is essential in protein homology modeling and in optimizing biologically active peptide ligands in medicinal chemistry. Furthermore, the tool of N-methylation of peptides is of increasing importance for the design of peptidic drugs to gain oral availability or receptor selectivity. However, N-methylation is often accompanied by considerable population of cis-peptide bond structures, resulting in completely different conformations compared with the parent peptide. To retain a favored structure, it might be important to understand the effect of different side chains on the backbone conformation and to enable the introduction of an N-methylation at the right position without disturbing a biologically active conformation. In order to detect even small energetic effects due to side chain mutations, we employed a trick to investigate the structural equilibrium of a selected cyclic pentapeptide in which two conformations are equally populated. Very small energetic differences between both conformations could easily be determined experimentally by identifying shifts in the population of both isomers.
dc.format.extent6 p.
dc.language.isoeng
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 Spain
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/es/
dc.subjectÀrees temàtiques de la UPC::Enginyeria dels materials
dc.subject.lcshPeptides--therapeutic use
dc.subject.lcshProtein engineering
dc.subject.otheramino acids
dc.subject.otherconformation analysis
dc.subject.othermethylation
dc.subject.otherpeptides
dc.subject.otherspatial screening
dc.titleThe impact of amino acid side chain mutations in conformational design of peptides and proteins
dc.typeArticle
dc.subject.lemacPèptids
dc.subject.lemacProteïnes
dc.contributor.groupUniversitat Politècnica de Catalunya. BIBITE - Biomaterials, Biomecànica i Enginyeria de Teixits
dc.identifier.doi10.1002/chem.201000545
dc.description.peerreviewedPeer Reviewed
dc.relation.publisherversionhttp://onlinelibrary.wiley.com/doi/10.1002/chem.201000545/abstract
dc.rights.accessRestricted access - publisher's policy
drac.iddocument15140647
dc.description.versionPostprint (published version)
dc.date.lift10000-01-01
upcommons.citation.authorLaufer, B.; Frank, A.; Chatterjee, J.; Neubauer, T.; Mas-Moruno, C.; Kummerlöwe, G.; Kessler, H.
upcommons.citation.publishedtrue
upcommons.citation.publicationNameChemistry: a european journal
upcommons.citation.volume16
upcommons.citation.number18
upcommons.citation.startingPage5385
upcommons.citation.endingPage5390
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Salvo que se indique lo contrario, los contenidos de esta obra estan sujetos a la licencia de Creative Commons: Reconocimiento-NoComercial-SinObraDerivada 3.0 España