2011
DOI: 10.1002/pro.561
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The role of the local environment of engineered Tyr to Trp substitutions for probing the denaturation mechanism of FIS

Abstract: Factor for inversion stimulation (FIS), a 98-residue homodimeric protein, does not contain tryptophan (Trp) residues but has four tyrosine (Tyr) residues located at positions 38, 51, 69, and 95. The equilibrium denaturation of a P61A mutant of FIS appears to occur via a three-state (N 2 I 2 2U) process involving a dimeric intermediate (I 2 ). Although it was suggested that this intermediate had a denatured C-terminus, direct evidence was lacking. Therefore, three FIS double mutants, P61A/Y38W, P61A/Y69W, and P… Show more

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Cited by 5 publications
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“…1 and 2). Unlike Trp fluorescence, the position of maximal emission of Tyr residues is insensitive to the polarity of the environment, consequently intensity of Tyr fluorescence has been used to monitor the structural alterations of insulin molecules [54,60].…”
Section: Resultsmentioning
confidence: 99%
“…1 and 2). Unlike Trp fluorescence, the position of maximal emission of Tyr residues is insensitive to the polarity of the environment, consequently intensity of Tyr fluorescence has been used to monitor the structural alterations of insulin molecules [54,60].…”
Section: Resultsmentioning
confidence: 99%