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http://purl.uniprot.org/SHA-384/76BB62D74ED5EC44CE7BE6F8FDE82DFA02D2560725C7CCA2ECCDA59F43F3562B08C588CD7C1D2FFB802839C5479F2D94http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Annotation
http://purl.uniprot.org/SHA-384/76BB62D74ED5EC44CE7BE6F8FDE82DFA02D2560725C7CCA2ECCDA59F43F3562B08C588CD7C1D2FFB802839C5479F2D94http://www.w3.org/2000/01/rdf-schema#comment"Data suggest that disulfide bonds can alter mechanical stability of proteins in different ways depending on properties of system. Disulfide-bonded E coli FimG (minor component of type 1 fimbriae) undergoes a 30% increase in its mechanical stability compared with its reduced counterpart. Unfolding force of human titan I91 domain exhibits decrease of 15% relative to the wild-type form."xsd:string
http://purl.uniprot.org/uniprot/#_95F85E39306317BAB1EB31B01F1D2CB928CED79711397818218D19C6E3276528E5BF33DD78C9D84214981D498431AFE7http://www.w3.org/1999/02/22-rdf-syntax-ns#subjecthttp://purl.uniprot.org/SHA-384/76BB62D74ED5EC44CE7BE6F8FDE82DFA02D2560725C7CCA2ECCDA59F43F3562B08C588CD7C1D2FFB802839C5479F2D94
http://purl.uniprot.org/uniprot/Q7Z3B7http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/76BB62D74ED5EC44CE7BE6F8FDE82DFA02D2560725C7CCA2ECCDA59F43F3562B08C588CD7C1D2FFB802839C5479F2D94
http://purl.uniprot.org/uniprot/#_Q7Z3B7-mappedCitation-28642368http://purl.uniprot.org/core/mappedAnnotationhttp://purl.uniprot.org/SHA-384/76BB62D74ED5EC44CE7BE6F8FDE82DFA02D2560725C7CCA2ECCDA59F43F3562B08C588CD7C1D2FFB802839C5479F2D94