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Inside Cover: Modulation of Ultrafast Conformational Dynamics in Allosteric Interaction of Gal Repressor Protein with Different Operator DNA Sequences (ChemBioChem 7/2016)
Author(s) -
Choudhury Susobhan,
Naiya Gitashri,
Singh Priya,
Lemmens Peter,
Roy Siddhartha,
Pal Samir Kumar
Publication year - 2016
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201600127
Subject(s) - allosteric regulation , repressor , chemistry , dna , förster resonance energy transfer , dimer , biophysics , protein dynamics , fluorescence anisotropy , fluorescence , protein structure , gene , biology , biochemistry , physics , gene expression , organic chemistry , quantum mechanics , membrane , enzyme
The inside cover picture shows an essential dance for the flow of life. A combined approach involving picosecond‐resolved FRET and polarization‐gated fluorescence was used to explore differential ultrafast dynamics in the allosteric interaction of Gal‐repressor protein dimer (GalR) with different operator‐DNA sequences, namely O E and O I . The observation of faster C‐terminal dynamics in the dimer upon N‐terminal recognition with O I compared to those with O E raises the possibility that the key ultrafast timescales of the protein fluctuations are involved in the allosteric regulation of tetramerization of the DNA‐bound dimers for a higher‐order nucleoprotein complex; this is likely to have functional consequences for regulating gene expression. More information can be found in the full paper by P. Lemmens, S. K. Pal et al. on page 605 in Issue 7, 2016 (DOI: 10.1002/cbic.201500657).