| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10803752 | Biochimie | 2013 | 10 Pages |
Abstract
⺠PIMT in Vibrio cholerae is functionally active. ⺠Biophysical characterization reveals a non-native intermediate in folding pathway. ⺠PIMT has different affinities for AdoMet and AdoHcy, both stabilizing the protein. ⺠Modeling and MD simulations also confirm higher stability of PIMT with cofactors. ⺠Osmolytes shift the unfolding equilibrium toward the native state.
Keywords
4,4′-dianilino-1,1′-binaphthyl-5,5′-disulfonic acidITCS-adenosyl homocysteineAdoMetAdoHcyDLSTMAOGdnHClS-adenosyl methioninePIMTOsmolytesFluorescence resonance energy transferFRETBis-ANSTrimethylamine N-oxidecircular dichroismFolding intermediateMethyltransferaseDynamic Light ScatteringIsothermal titration calorimetry
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Authors
Tanaya Chatterjee, Aritrika Pal, Devlina Chakravarty, Sucharita Dey, Rudra P. Saha, Pinak Chakrabarti,