scholarly journals Physical origin of hydrophobicity studied in terms of cold denaturation of proteins: comparison between water and simple fluids

2012 ◽  
Vol 14 (42) ◽  
pp. 14554 ◽  
Author(s):  
Takashi Yoshidome ◽  
Masahiro Kinoshita
Keyword(s):  
Physical Origin ◽  
Simple Fluids ◽  
Cold Denaturation ◽  
Denaturation Of Proteins

Heightened Cold-Denaturation of Proteins at the Ice–Water Interface

2020 ◽  
Vol 142 (12) ◽  
pp. 5722-5730 ◽  
Author(s):  
Andrea Arsiccio ◽  
James McCarty ◽  
Roberto Pisano ◽  
Joan-Emma Shea
Keyword(s):  
Water Interface ◽  
Cold Denaturation ◽  
Ice Water ◽  
Denaturation Of Proteins

scholarly journals The role of hydrophobicity in the cold denaturation of proteins under high pressure: A study on apomyoglobin

2019 ◽  
Vol 150 (7) ◽  
pp. 075102 ◽  
Author(s):  
Yanis R. Espinosa ◽  
Ernesto R. Caffarena ◽  
J. Raúl Grigera
Keyword(s):  
High Pressure ◽  
Cold Denaturation ◽  
Denaturation Of Proteins

scholarly journals Heat, Cold and Pressure Induced Denaturation of Proteins

2003 ◽  
Vol 17 (2-3) ◽  
pp. 367-376 ◽  
Author(s):  
G. Panick ◽  
H. Herberhold ◽  
Z. Sun ◽  
R. Winter
Keyword(s):  
Infrared Spectroscopy ◽  
Secondary Structure ◽  
Structural Properties ◽  
Relaxation Technique ◽  
Cold Denaturation ◽  
Unfolded State ◽  
Fouriertransform Infrared Spectroscopy ◽  
Monomeric Proteins ◽  
Kinetics Of ◽  
Denaturation Of Proteins

We studied the pressureinduced unfolding and refolding of monomeric proteins, such as SNase, αchymotrypsin and ubiquitin, by using synchrotron Xray smallangle scattering and Fouriertransform infrared spectroscopy, which monitor changes in the tertiary and secondary structural properties of the proteins upon pressurization. Furthermore, by using the pressurejump relaxation technique in combination with timeresolved Xray diffraction and infrared spectroscopy, the kinetics of the unfolding/refolding of the proteins, was investigated. Significant differences in secondary structure and chain compactness in the folding/unfolding reactions of these proteins are observed. The results are compared with data obtained from other methods of denaturation, such as heat and pressure-assisted cold denaturation. The cold- and pressure-induced unfolding both yield a particularly unfolded state characterized by a persistent amount of secondary structure.

Hot and cold denaturation of proteins: Critical aspects

1999 ◽  
Vol 10 (1) ◽  
pp. 193-196 ◽  
Author(s):  
A. Hansen ◽  
M.H. Jensen ◽  
K. Sneppen ◽  
G. Zocchi
Keyword(s):  
Cold Denaturation ◽  
Denaturation Of Proteins ◽  
Critical Aspects

scholarly journals Implicit water model within the Zimm-Bragg approach to analyze experimental data for heat and cold denaturation of proteins

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Artem Badasyan ◽  
Shushanik Tonoyan ◽  
Matjaz Valant ◽  
Joze Grdadolnik
Keyword(s):  
Experimental Data ◽  
Degrees Of Freedom ◽  
Hamiltonian Formulation ◽  
Theoretical Models ◽  
Water Model ◽  
Explicit Model ◽  
Significant Progress ◽  
Cold Denaturation ◽  
Denaturation Of Proteins

AbstractStudies of biopolymer conformations essentially rely on theoretical models that are routinely used to process and analyze experimental data. While modern experiments allow study of single molecules in vivo, corresponding theories date back to the early 1950s and require an essential update to include the recent significant progress in the description of water. The Hamiltonian formulation of the Zimm-Bragg model we propose includes a simplified, yet explicit model of water-polypeptide interactions that transforms into the equivalent implicit description after performing the summation of solvent degrees of freedom in the partition function. Here we show that our model fits very well to the circular dichroism experimental data for both heat and cold denaturation and provides the energies of inter- and intra-molecular H-bonds, unavailable with other processing methods. The revealed delicate balance between these energies determines the conditions for the existence of cold denaturation and thus clarifies its absence in some proteins.

Sign in / Sign up

Export Citation Format

Share Document