scholarly journals Effects of Monovalent Anions on a Temperature-Dependent Heat Capacity Change forEscherichia coliSSB Tetramer Binding to Single-Stranded DNA†

Biochemistry ◽  
2006 ◽  
Vol 45 (16) ◽  
pp. 5190-5205 ◽  
Author(s):  
Alexander G. Kozlov ◽  
Timothy M. Lohman
Keyword(s):  
Heat Capacity ◽  
Heat Capacity Change ◽  
Temperature Dependent ◽  
Single Stranded Dna ◽  
Tetramer Binding ◽  
Capacity Change

scholarly journals Thermodynamics and Intermolecular Interactions of Nicotinamide in Neat and Binary Solutions: Experimental Measurements and COSMO-RS Concentration Dependent Reactions Investigations

2021 ◽  
Vol 22 (14) ◽  
pp. 7365
Author(s):  
Piotr Cysewski ◽  
Maciej Przybyłek ◽  
Anna Kowalska ◽  
Natalia Tymorek
Keyword(s):  
Intermolecular Interactions ◽  
Vibrational Energy ◽  
Perfect Match ◽  
Zero Point ◽  
Heat Capacity Change ◽  
Free Energies ◽  
Temperature Dependent ◽  
Scanning Calorimetry ◽  
Capacity Change ◽  
Self Association

In this study, the temperature-dependent solubility of nicotinamide (niacin) was measured in six neat solvents and five aqueous-organic binary mixtures (methanol, 1,4-dioxane, acetonitrile, DMSO and DMF). It was discovered that the selected set of organic solvents offer all sorts of solvent effects, including co-solvent, synergistic, and anti-solvent features, enabling flexible tuning of niacin solubility. In addition, differential scanning calorimetry was used to characterize the fusion thermodynamics of nicotinamide. In particular, the heat capacity change upon melting was measured. The experimental data were interpreted by means of COSMO-RS-DARE (conductor-like screening model for realistic solvation–dimerization, aggregation, and reaction extension) for concentration dependent reactions. The solute–solute and solute–solvent intermolecular interactions were found to be significant in all of the studied systems, which was proven by the computed mutual affinity of the components at the saturated conditions. The values of the Gibbs free energies of pair formation were derived at an advanced level of theory (MP2), including corrections for electron correlation and zero point vibrational energy (ZPE). In all of the studied systems the self-association of nicotinamide was found to be a predominant intermolecular complex, irrespective of the temperature and composition of the binary system. The application of the COSMO-RS-DARE approach led to a perfect match between the computed and measured solubility data, by optimizing the parameter of intermolecular interactions.

scholarly journals Heat capacity change for ribonuclease A folding

1999 ◽  
Vol 8 (7) ◽  
pp. 1500-1504 ◽  
Author(s):  
C. Nick Pace ◽  
Gerald R. Grimsley ◽  
Susan T. Thomas ◽  
George I. Makhatadze
Keyword(s):  
Heat Capacity ◽  
Ribonuclease A ◽  
Heat Capacity Change ◽  
Capacity Change

scholarly journals Temperature control technology by heat capacity change upon lock and key binding

2010 ◽  
Vol 375 (2) ◽  
pp. 165-169 ◽  
Author(s):  
Ken-ichi Amano ◽  
Daisuke Miyazaki ◽  
Liew Fong Fong ◽  
Paul Hilscher ◽  
Taro Sonobe
Keyword(s):  
Heat Capacity ◽  
Temperature Control ◽  
Heat Capacity Change ◽  
Control Technology ◽  
Capacity Change

scholarly journals Thermodynamics of DNA: heat capacity changes on duplex unfolding

2019 ◽  
Vol 48 (8) ◽  
pp. 773-779 ◽  
Author(s):  
Anatoliy Dragan ◽  
Peter Privalov ◽  
Colyn Crane-Robinson
Keyword(s):  
Heat Capacity ◽  
Accessible Surface Area ◽  
Solvent Accessible Surface Area ◽  
Polar Component ◽  
Heat Capacity Change ◽  
Dna Duplex ◽  
Capacity Change ◽  
Heat Capacity Changes ◽  
Accessible Surface ◽  
Lower Magnitude

Abstract The heat capacity change, ΔCp, accompanying the folding/unfolding of macromolecules reflects their changing state of hydration. Thermal denaturation of the DNA duplex is characterized by an increase in ΔCp but of much lower magnitude than observed for proteins. To understand this difference, the changes in solvent accessible surface area (ΔASA) have been determined for unfolding the B-form DNA duplex into disordered single strands. These showed that the polar component represents ~ 55% of the total increase in ASA, in contrast to globular proteins of similar molecular weight for which the polar component is only about 1/3rd of the total. As the exposure of polar surface results in a decrease of ΔCp, this explains the much reduced heat capacity increase observed for DNA and emphasizes the enhanced role of polar interactions in maintaining duplex structure. Appreciation of a non-zero ΔCp for DNA has important consequences for the calculation of duplex melting temperatures (Tm). A modified approach to Tm prediction is required and comparison is made of current methods with an alternative protocol.

Heat capacity change on isothermal vitrification during a macromolecule's growth

1993 ◽  
Vol 201 (1-3) ◽  
pp. 95-100 ◽  
Author(s):  
M. Cassettari ◽  
G. Salvetti ◽  
E. Tombari ◽  
S. Veronesi ◽  
G.P. Johari
Keyword(s):  
Heat Capacity ◽  
Heat Capacity Change ◽  
Capacity Change

scholarly journals Glucosylation of β-lactoglobulin lowers the heat capacity change of unfolding; a unique way to affect protein thermodynamics

2005 ◽  
Vol 14 (8) ◽  
pp. 2187-2194 ◽  
Author(s):  
Annemarie M.M. Van Teeffelen ◽  
Kerensa Broersen ◽  
Harmen H.J. de Jongh
Keyword(s):  
Heat Capacity ◽  
Heat Capacity Change ◽  
Protein Thermodynamics ◽  
Capacity Change ◽  
Β Lactoglobulin

Contrasting Effects of Salt and Temperature on Niosome-Bound Norharmane: Direct Evidence for Positive Heat Capacity Change in the Niosome:β-Cyclodextrin Interaction

2016 ◽  
Vol 120 (17) ◽  
pp. 4091-4101 ◽  
Author(s):  
Bijan K. Paul ◽  
Narayani Ghosh ◽  
Ramakanta Mondal ◽  
Saptarshi Mukherjee
Keyword(s):  
Heat Capacity ◽  
Direct Evidence ◽  
Heat Capacity Change ◽  
Capacity Change
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