1999
Using loop length variants to dissect the folding pathway of a four-helix-bundle protein 11Edited by P. E. Wright
Nagi A, Anderson K, Regan L. Using loop length variants to dissect the folding pathway of a four-helix-bundle protein 11Edited by P. E. Wright. Journal Of Molecular Biology 1999, 286: 257-265. PMID: 9931264, DOI: 10.1006/jmbi.1998.2474.Peer-Reviewed Original ResearchMeSH KeywordsEscherichia coliKineticsMutationProtein DenaturationProtein FoldingProtein Structure, SecondaryRecombinant ProteinsConceptsFour-helix bundle proteinWild-type proteinHelix-connecting loopsProtein folding pathwaysMutant proteinsTwo-residue loopSame general mechanismHelix monomersLength variantsFolding pathwaysE. WrightDimeric intermediateProteinGeneral mechanismFoldingPolyglycine linkerPathwayGlycine linkerLinkerLoop lengthAlterations
1996
Surface point mutations that significantly alter the structure and stability of a protein's denatured state
Smith C, Bu Z, Engelman D, Regan L, Anderson K, Sturtevant J. Surface point mutations that significantly alter the structure and stability of a protein's denatured state. Protein Science 1996, 5: 2009-2019. PMID: 8897601, PMCID: PMC2143264, DOI: 10.1002/pro.5560051007.Peer-Reviewed Original ResearchConceptsPoint mutationsDenatured stateStopped-flow fluorescenceDenaturant concentrationSolvent-exposed sitesStreptococcal protein GMutantsG mutantTertiary structureGuHCl denaturationEquilibrium intermediatesPosition 53B1 domainProteinCircular dichroismMutationsProtein GGuanidine hydrochlorideSmall-angle X-ray scatteringStructural implicationsX-ray scatteringFluorescenceThrRadius of gyrationDenaturants