Transfer Free Energies of Test Proteins Into Crowded Protein Solutions Have Simple Dependence on Crowder Concentration
The effects of macromolecular crowding on the thermodynamic properties of test proteins are determined by the latter's transfer free energies from a dilute solution to a crowded solution. The transfer free energies in turn are determined by effective protein-crowder interactions. When these int...
Main Authors: | Valery Nguemaha, Sanbo Qin, Huan-Xiang Zhou |
---|---|
Format: | Article |
Language: | English |
Published: |
Frontiers Media S.A.
2019-05-01
|
Series: | Frontiers in Molecular Biosciences |
Subjects: | |
Online Access: | https://www.frontiersin.org/article/10.3389/fmolb.2019.00039/full |
Similar Items
-
Carbohydrate-Based Macromolecular Crowding-Induced Stabilization of Proteins: Towards Understanding the Significance of the Size of the Crowder
by: Sumra Shahid, et al.
Published: (2019-09-01) -
Investigation on the effect of nonpolar amino acids as macromolecular crowders on the stability of globular proteins
by: Saikat Pal, et al.
Published: (2022-06-01) -
Organization of the bacterial nucleoid by DNA-bridging proteins and globular crowders
by: Marc Joyeux
Published: (2023-02-01) -
Structural Refolding and Thermal Stability of Myoglobin in the Presence of Mixture of Crowders: Importance of Various Interactions for Protein Stabilization in Crowded Conditions
by: Zahoor Ahmad Parray, et al.
Published: (2021-05-01) -
Modeling Crowded Environment in Molecular Simulations
by: Natalia Ostrowska, et al.
Published: (2019-09-01)