alpha and beta Conformational preferences in fibril forming peptides characterised using NMR and CD techniques

dc.creatorPertinhez, TA
dc.creatorSherwood, AK
dc.creatorFraceto, LF
dc.creatorBouchard, M
dc.creatorPitkeathly, M
dc.creatorSmith, LJ
dc.date2004
dc.date2014-08-01T18:19:18Z
dc.date2015-11-26T18:01:43Z
dc.date2014-08-01T18:19:18Z
dc.date2015-11-26T18:01:43Z
dc.date.accessioned2018-03-29T00:43:21Z
dc.date.available2018-03-29T00:43:21Z
dc.identifierSpectroscopy-an International Journal. Ios Press, v. 18, n. 1, n. 1, n. 11, 2004.
dc.identifier0712-4813
dc.identifierWOS:000188544700001
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/77165
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/77165
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1292056
dc.descriptionPeptide fragments taken from residues 18-54 of short consensus repeat 3 (SCR3) from the human complement receptor CR1 have been found in aqueous solution to slowly aggregate and form fibrils. NMR studies of the monomeric form of these peptides show that they are essentially unfolded in aqueous solution and that they all have an increased helicity in TFE solutions. The behaviour of residues 28-31 from SCR3 is particularly interesting. These residues have a high beta-sheet propensity in the native protein and a seven peptide containing their sequence is found to form fibrils despite its short length. However, NMR studies show that these residues adopt a well-defined alpha-helix in 80% TFE and under these conditions fibril formation has not been observed. These data demonstrate the strong dependence of conformational propensities on environment.
dc.description18
dc.description1
dc.description1
dc.description11
dc.languageen
dc.publisherIos Press
dc.publisherAmsterdam
dc.publisherHolanda
dc.relationSpectroscopy-an International Journal
dc.relationSpectr.-Int. J.
dc.rightsfechado
dc.rightshttp://www.iospress.nl/service/authors/author-copyright-agreement/
dc.sourceWeb of Science
dc.subjectProtein Secondary Structure
dc.subjectChemical-shifts
dc.subjectRandom Coil
dc.subjectDenatured Proteins
dc.subjectResidual Structure
dc.subjectGlobular Protein
dc.subjectAmyloid Fibrils
dc.subjectAmino-acids
dc.subjectTrifluoroethanol
dc.subjectSpectroscopy
dc.titlealpha and beta Conformational preferences in fibril forming peptides characterised using NMR and CD techniques
dc.typeArtículos de revistas


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