Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/15817
Title: Structural and equilibrium unfolding studies of sam domain of DLC1 by NMR spectroscopy
Authors: YANG SHUAI
Keywords: Structure, Equilibrium Unfolding, NMR
Issue Date: 24-Apr-2009
Source: YANG SHUAI (2009-04-24). Structural and equilibrium unfolding studies of sam domain of DLC1 by NMR spectroscopy. ScholarBank@NUS Repository.
Abstract: We have determined the solution structure of DLC1-SAM using triple resonance NMR techniques. The solution structure of DLC1-SAM provides a basis for the determination of potential residues that are involved in interactions with a novel binding partner, EF1A1, of the SAM superfamily. We also investigated the equilibrium unfolding of DLC1-SAM with various biophysical methods such as CD, fluorescence emission spectroscopy and NMR. CD and tryptophan intrinsic fluorescence emission data imply that the unfolding of DLC1-SAM follows a simple two-state mechanism; yet the NMR data suggest the presence of at least one intermediate state. The intermediate is undetectable by NMR, but it does not exist in large aggregates as shown by analytical ultracentrifugation experiments.
URI: http://scholarbank.nus.edu.sg/handle/10635/15817
Appears in Collections:Ph.D Theses (Open)

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