On the difference in stability between horse and sperm whale myoglobins

dc.creatorRegis, WCB
dc.creatorFattori, J
dc.creatorSantoro, MM
dc.creatorJamin, M
dc.creatorRamos, CHI
dc.date2005
dc.dateAPR 1
dc.date2014-11-14T03:25:15Z
dc.date2015-11-26T17:12:57Z
dc.date2014-11-14T03:25:15Z
dc.date2015-11-26T17:12:57Z
dc.date.accessioned2018-03-29T00:01:21Z
dc.date.available2018-03-29T00:01:21Z
dc.identifierArchives Of Biochemistry And Biophysics. Elsevier Science Inc, v. 436, n. 1, n. 168, n. 177, 2005.
dc.identifier0003-9861
dc.identifierWOS:000227685000020
dc.identifier10.1016/j.abb.2005.01.016
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/68640
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/68640
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/68640
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1281456
dc.descriptionThe work in the literature on apomyoglobin is almost equally divided between horse and sperm whale myoglobins. The two proteins share high homology, show similar folding behavior, and it is often assumed that all folding phenomena found with one protein will also be found with the other. We report data at equilibrium showing that horse myoglobin was 2.1 kcal/mol less stable than sperm whale myoglobin at pH 5.0 and aggregated at high concentrations as measured by gel filtration and analytical ultracentrifugation experiments. The higher stability of sperm whale myoglobin was identified for both apo and holo forms, and was independent of pH from 5 to 8 and of the presence of sodium chloride. We also show that the substitution of sperm whale myoglobin residues Ala 15 and Ala74 to Gly, the residues found at positions 15 and 74 in horse myoglobin, decreased the stability by 1.0 kcal/mol, indicating that helix propensity is an important component of the explanation for the difference in stability between the two proteins. (c) 2005 Elsevier Inc. All rights reserved.
dc.description436
dc.description1
dc.description168
dc.description177
dc.languageen
dc.publisherElsevier Science Inc
dc.publisherNew York
dc.publisherEUA
dc.relationArchives Of Biochemistry And Biophysics
dc.relationArch. Biochem. Biophys.
dc.rightsfechado
dc.rightshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.sourceWeb of Science
dc.subjectprotein stability
dc.subjectprotein folding
dc.subjectmyoglobin
dc.subjectanalytical ultracentrifugation
dc.subjectalpha-helix
dc.subjectsite-directed mutagenesis
dc.subjectMolten Globule Intermediate
dc.subjectAlpha-helices
dc.subjectProtein Stability
dc.subjectStructural-characterization
dc.subjectFolding Pathway
dc.subjectRibonuclease-a
dc.subjectHeme-proteins
dc.subjectApomyoglobin
dc.subjectDynamics
dc.subjectPropensities
dc.titleOn the difference in stability between horse and sperm whale myoglobins
dc.typeArtículos de revistas


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