ASM 2019

Invited Talk (I6)

9/3/2019, 4:15 pm - 4:45 pm in LH 310


Prof. Parbati Biswas

Dept. of Chemistry, Univ. of Delhi,

Delhi-110007

E-mail: pbiswas[at]chemistry.du.ac.in

 

HYDRATION PATTERN OF INTRINSICALLY DISORDERED PROTEINS

Intrinsically disordered proteins lack a unique three-dimensional tertiary structure either entirely or partially and exist as dynamic ensemble of interconvertible conformations under standard physiological conditions. Analysis of the hydration capacity reveals that the disordered proteins have a larger binding capacity for hydration water as compared to the globular proteins. The surface and radial distributions of the water molecules also confirm this trend. The local structure of the hydration water evaluated in terms of the tetrahedral order parameter depicts a higher order among water molecules surrounding the disordered proteins/regions. The orientation of the water molecules is distinctly different for the ordered and disordered proteins/regions. Enhanced hydration water mobility in the vicinity of the disordered proteins/regions is related to their high hydration capacity, low hydrophobicity and increased internal motions.

References:

[1] Aggarwal L; Biswas P. J. Phys. Chem. B 122, 4206, 2018

[2] Baruah A.; Biswas P. Phys. Chem. Chem. Phys. 18, 23207, 2016.

[3] Baruah, A.; Rani, P.; Biswas, P. Sci. Rep. 5, 11740, 2015.

[4] Rani P; Biswas P. J. Phys. Chem. B 119, 13262, 2015

[5] Rani P; Biswas P. J. Phys. Chem. B 119, 10858, 2015

Invited Speakers Program