01853nas a2200265   4500008004100000022001400041245011100055210006900166260006900235300001000304490000800314520088600322653002701208653005001235653001501285653001801300653002201318653001501340100001701355700001801372700002701390700001901417700002001436856013101456       2011                        eng d  a1011-134400aFluorescence resonance energy transfer from tryptophan to folic acid in micellar media and deionised water0 aFluorescence resonance energy transfer from tryptophan to folic   aPO BOX 564, 1001 LAUSANNE, SWITZERLANDbELSEVIER SCIENCE SAcAPR  a16-210 v1033 a<p>The fluorescence resonance energy transfer (FRET) from tryptophan (Trp) to folic acid (FA) in aqueous sodiumdodecyl sulphate, cetyltrimethyl ammonium bromide, and Brij-35 as well as deionised water was investigated using steady state and time resolved fluorescence techniques. The data obtained from steady state fluorescence spectral studies and time resolved measurement indicated that the FRET from Trp to FA occurred most effectively in aqueous sodium dodecyl sulphate micellar solutions. The distance between Trp and FA were evaluated. Binding constant, number of binding sites and thermodynamic parameters were determined for Trp-FA interactions in deionised water. The values of the thermodynamic parameters suggest that the hydrophobic forces and hydrogen bonding are the key interacting forces between Trp-FA interaction. (C) 2011 Elsevier B.V. All rights reserved.</p>10aFluorescence quenching10aFluorescence resonance energy transfer (FRET)10aFolic acid10aFoster theory10aStern-Volmer plot10aTryptophan1 aMote, U., S.1 aPatil, S., R.1 aBhosale, Siddharth, H.1 aHan, Sung-Hwan1 aKolekar, G., B.  uhttps://library.ncl.res.in/content/fluorescence-resonance-energy-transfer-tryptophan-folic-acid-micellar-media-and-deionised-002418nas a2200253   4500008004100000022001400041245010700055210006900162260007300231300001200304490000700316520147800323653001601801653002001817653002701837653004101864653001401905100002101919700001801940700002701958700002701985700002502012856012702037       2016                        eng d  a0141-813000aFunctional and conformational transitions of mevalonate diphosphate decarboxylase from Bacopa monniera0 aFunctional and conformational transitions of mevalonate diphosph  aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcFEB  a160-1700 v833 a<p>Functional and conformational transitions of mevalonate diphosphate decarboxylase (MDD), a key enzyme of mevalonate pathway in isoprenoid biosynthesis, from Bacopa monniera (BmMDD), cloned and overexpressed in Escherichia coli were studied under thermal, chemical and pH-mediated denaturation conditions using fluorescence and Circular dichroism spectroscopy. Native BmMDD is a helix dominant structure with 45% helix and 11% sheets and possesses seven tryptophan residues with two residues exposed on surface, three residues partially exposed and two situated in the interior of the protein. Thermal denaturation of BmMDD causes rapid structural transitions at and above 40 degrees C and transient exposure of hydrophobic residues at 50 degrees C, leading to aggregation of the protein. An acid induced molten globule like structure was observed at pH 4, exhibiting altered but compact secondary structure, distorted tertiary structure and exposed hydrophobic residues. The molten globule displayed different response at higher temperature and similar response to chemical denaturation as compared to the native protein. The surface tryptophans have predominantly positively charged amino acids around them, as indicated by higher K-SV for IC as compared to that for CsCl. The native enzyme displayed two different lifetimes, vi (1.203 +/- 0.036 ns) and tau 2 (3.473 +/- 0.12 ns) indicating two populations of tryptophan. (C) 2015 Elsevier B.V. All rights reserved.</p>10aAggregation10aCD spectroscopy10aFluorescence quenching10aMevalonate diphosphate decarboxylase10aUnfolding1 aShakeel, Abbassi1 aPatel, Krunal1 aKhan, Bashir, Mohammad1 aBhosale, Siddharth, H.1 aGaikwad, Sushama, M.  uhttps://library.ncl.res.in/content/functional-and-conformational-transitions-mevalonate-diphosphate-decarboxylase-bacopa-0