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http://purl.uniprot.org/citations/10684603http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10684603http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10684603http://www.w3.org/2000/01/rdf-schema#comment"The role of surface salt bridges in protein stabilization has been a source of controversy. Here we present the NMR structure of a hyperthermophilic rubredoxin variant (PFRD-XC4) and the thermodynamic analysis of two surface salt bridges by double mutant cycles. This analysis shows that the surface side chain to side chain salt bridge between Lys 6 and Glu 49 does not stabilize PFRD-XC4. The main chain to side chain salt bridge between the N-terminus and Glu 14 was, however, found to stabilize PFRD-XC4 by 1. 5 kcal mol(-)(1). The entropic cost of making a surface salt bridge involving the protein's backbone is reduced, since the backbone has already been immobilized upon protein folding."xsd:string
http://purl.uniprot.org/citations/10684603http://purl.org/dc/terms/identifier"doi:10.1021/bi992257j"xsd:string
http://purl.uniprot.org/citations/10684603http://purl.org/dc/terms/identifier"doi:10.1021/bi992257j"xsd:string
http://purl.uniprot.org/citations/10684603http://purl.uniprot.org/core/author"Strop P."xsd:string
http://purl.uniprot.org/citations/10684603http://purl.uniprot.org/core/author"Strop P."xsd:string
http://purl.uniprot.org/citations/10684603http://purl.uniprot.org/core/author"Mayo S.L."xsd:string
http://purl.uniprot.org/citations/10684603http://purl.uniprot.org/core/author"Mayo S.L."xsd:string
http://purl.uniprot.org/citations/10684603http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10684603http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10684603http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/10684603http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/10684603http://purl.uniprot.org/core/pages"1251-1255"xsd:string
http://purl.uniprot.org/citations/10684603http://purl.uniprot.org/core/pages"1251-1255"xsd:string
http://purl.uniprot.org/citations/10684603http://purl.uniprot.org/core/title"Contribution of surface salt bridges to protein stability."xsd:string
http://purl.uniprot.org/citations/10684603http://purl.uniprot.org/core/title"Contribution of surface salt bridges to protein stability."xsd:string
http://purl.uniprot.org/citations/10684603http://purl.uniprot.org/core/volume"39"xsd:string
http://purl.uniprot.org/citations/10684603http://purl.uniprot.org/core/volume"39"xsd:string
http://purl.uniprot.org/citations/10684603http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10684603
http://purl.uniprot.org/citations/10684603http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10684603
http://purl.uniprot.org/citations/10684603http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10684603
http://purl.uniprot.org/citations/10684603http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10684603
http://purl.uniprot.org/uniprot/P24297http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/10684603
http://purl.uniprot.org/uniprot/#_P24297-citation-10684603http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/10684603