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Solvation Dynamics of a Protein in the Pre Molten Globule State

IR@IICB: CSIR-Indian Institute of Chemical Biology, Kolkata

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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/