1995
DOI: 10.1021/bi00008a040
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Abstract: The rat intestinal fatty acid binding protein is an almost all beta-sheet protein that encloses a large interior cavity into which the fatty acid ligand binds. The protein contains neither cysteine nor proline. In a previous report, six site-directed mutants were obtained, each having a single cysteine residue [Jiang, N., & Frieden, C., (1993) Biochemistry 32, 11015-11021] either in a turn or pointed into the cavity. In this report, each mutant has been unfolded in denaturant and modified with 5-iodoacetamido-… Show more

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Cited by 27 publications
(20 citation statements)
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References 21 publications
(31 reference statements)
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“…The stability of both the mutants is similar with identical mid-points (Table 1). It can be seen that a large fluorescence change occurs with the V60Flu protein on unfolding which indicates that the fluorescein is inside the cavity consistent with earlier NMR data using V60Flu (13). The different behavior for F62Flu (Fig.…”
Section: Resultssupporting
confidence: 87%
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“…The stability of both the mutants is similar with identical mid-points (Table 1). It can be seen that a large fluorescence change occurs with the V60Flu protein on unfolding which indicates that the fluorescein is inside the cavity consistent with earlier NMR data using V60Flu (13). The different behavior for F62Flu (Fig.…”
Section: Resultssupporting
confidence: 87%
“…Equilibrium unfolding experiments using different cysteine modified mutants of IFABP have been studied earlier (12,13). Unfolding of mutant proteins with fluorescein attached to positions 60, 89, and 104 was accompanied by a significant increase in fluorescence intensity at 517 nm (excitation wavelength of 490 nm).…”
Section: Resultsmentioning
confidence: 99%
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