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Solvation Dynamics of a Protein in the Pre Molten Globule State

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Title Solvation Dynamics of a Protein in the Pre Molten Globule State
 
Creator Samaddar, Soma
Mandal, Amit Kumar
Mondal, Sudip Kumar
Sahu, Kalyanasis
Bhattacharyya, Kankan
Roy, Siddhartha
 
Subject Structural Biology & Bioinformatics
 
Description The nature of solvent molecules around proteins in native and different non-native states is crucial for
understanding the protein folding problem. We have characterized two compact denatured states of glutaminyltRNA
synthetase (GlnRS) under equilibrium conditions in the presence of a naturally occurring osmolyte,
L-glutamate. The solvation dynamics of the compact denatured states and the fully unfolded state has been
studied using a covalently attached probe, acrylodan, near the active site. The solvation dynamics progressively
becomes faster as the protein goes from the native to the molten globule to the pre molten globule to the fully
unfolded state. Anisotropy decay measurements suggest that the pre-molten-globule intermediate is more
flexible than the molten globule although the secondary structure is largely similar. Dynamic light scattering
studies reveal that both the compact denatured states are aggregated under the measurement conditions. The
implications of solvation dynamics in aggregated compact denatured states have been discussed.
 
Publisher American Chemical Society
 
Date 2005
 
Type Article
PeerReviewed
 
Format application/pdf
 
Identifier http://www.eprints.iicb.res.in/409/1/JOURNAL_OF_PHYSICAL_CHEMISTRY_B%2C_110(42)%2C_21210%2D21215%2C[23].pdf
Samaddar, Soma and Mandal, Amit Kumar and Mondal, Sudip Kumar and Sahu, Kalyanasis and Bhattacharyya, Kankan and Roy, Siddhartha (2005) Solvation Dynamics of a Protein in the Pre Molten Globule State. The Journal of Physical Chemistry B, 110 (42). pp. 21210-21215.
 
Relation http://dx.doi.org/10.1021/jp064136g CCC: $33.50
http://www.eprints.iicb.res.in/409/