Partial molar volumes, expansibilities, and compressibilities of oligoglycines in aqueous solutions at 18–55°C

Chalikian, Tigran V.; Sarvazyan, Armen; Funck, Theodor; Breslauer, Kenneth J.

doi:10.1002/bip.360340409

Cited by 87 publications

(78 citation statements)

References 44 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Our standard state data for this system are in very good agreement with the averaged apparent molar volumes reported as a function of temperature in a recent paper by Chalikian et al (5).…”

Section: Resultssupporting

confidence: 91%

See 1 more Smart Citation

Calorimetric investigations of aqueous amino acid and dipeptide systems from 288. 15 to 328. 15 K

Hakin¹,

Duke²,

Groft³

et al. 1995

Can. J. Chem.

100

View full text Add to dashboard Cite

Densities and heat capacities have been measured for aqueous solutions of L-asparagine, L-glutamine, glycylglycine, glycyl-L-valine, glycyl-L-asparagine, and glycyl-DL-leucine at 288. 15,298.15, 313.15, and 328.15 K. These data have been used to calculate apparent molar volumes, V2,0, and apparent molar heat capacities, Cp,2,0, which in turn have been used to obtain standard state volumes, v;, and heat capacities, c;,,.The semi-empirical modelling procedures of Helgeson, Kirkham, and Flowers have been used to subdivide the calculated standard state volume and heat capacity data into solvation and nonsolvation contributions. The nonsolvation components of the standard state properties are used in group additivity analyses. These analyses yield structural contributions to standard state volumes and heat capacities for the CH(NH,)CO,H, CH,, OH, COOH, CH, CONH,, and CONH groups. The temperature dependences of these contributions are discussed. Some comments are reported concerning the practicality of using the thermodynamic properties of aqueous amino acid and peptide systems as the basis for modelling standard state thermodynamic properties of aqueous protein systems.Key words: heat capacities, densities, volumes, amino acids, peptides, group additivity. On rapporte quelques commentaires relatifs au caractere pratique de l'utilisation des propriCtCs thermodynamiques des systemes aqueux d'acides aminCs et de peptides pour la modClisation des propriCtCs thermodynamiques standard des systkmes aqueux de protkines.

show abstract

“…Our standard state data for this system are in very good agreement with the averaged apparent molar volumes reported as a function of temperature in a recent paper by Chalikian et al (5).…”

Section: Resultssupporting

confidence: 91%

“…Our analyses yield estimates of the contributions made by the CHNH,COOH, OH, COOH, CH,, CH, CONH,, and CONH groups. Equation [5] may therefore be written in the form:…”

Section: Group Additivity Analysesmentioning

confidence: 99%

Calorimetric investigations of aqueous amino acid and dipeptide systems from 288. 15 to 328. 15 K

Hakin¹,

Duke²,

Groft³

et al. 1995

Can. J. Chem.

100

View full text Add to dashboard Cite

show abstract

“…60 The volume and compressibility contributions of the glycyl residue determined in both ways are listed in Tables I and II, respectively. Inspection of Tables I and II reveals that the volume and compressibility contributions of the glycyl residue in N-acetyl glycine methylamide are significantly smaller than the respective contributions of the glycyl residue in oligoglycines.…”

Section: Volumetric Contributions Of Glycyl Residuementioning

confidence: 99%

Urea interactions with protein groups: A volumetric study

2010

Self Cite

View full text Add to dashboard Cite

We determined the partial molar volumes and adiabatic compressibilities of N-acetyl amino acid amides, N-acetyl amino acid methylamides, N-acetyl amino acids, and short oligoglycines as a function of urea concentration. We analyze these data within the framework of a statistical thermodynamic formalism to determine the association constants for the reaction in which urea binds to the glycyl unit and each of the naturally occurring amino acid side chains replacing two waters of hydration. Our determined association constants, k, range from 0.04 to 0.39 M. We derive a general equation that links k with changes in free energy, DeltaGtr, accompanying the transfer of functional groups from water to urea. In this equation, DeltaGtr is the sum of a change in the free energy of cavity formation, DeltaDeltaGC, and the differential free energy of solute-solvent interactions, DeltaDeltaGI, in urea and water. The observed range of affinity coefficients, k, corresponds to the values of DeltaDeltaGI ranging from highly favorable to slightly unfavorable. Taken together, our data support a direct interaction model in which urea denatures a protein by concerted action via favorable interactions with a wide range of protein groups. Our derived equation linking k to DeltaGtr suggests that DeltaDeltaGI and, hence, the net transfer free energy, DeltaGtr, are both strongly influenced by the concentration of a solute used in the experiment. We emphasize the need to exercise caution when two solutes differing in solubility are compared to determine the DeltaGtr contribution of a particular functional group.

show abstract

“…3,29,30,51,52 Thus, at least from the point of view of acousto-densimetric measurements, the "quantity" of the hydration shell of small molecules consists primarily of water molecules that contact a solute directly. However, for large molecules, this statement may not be true.…”

Section: Relationship Between Volumetric and Hydration Properties Of mentioning

confidence: 99%

The hydration of nucleic acid duplexes as assessed by a combination of volumetric and structural techniques

Chalikian¹,

Völker²,

Srinivasan³

et al. 1999

Biopolymers

Self Cite

View full text Add to dashboard Cite

Partial molar volumes, expansibilities, and compressibilities of oligoglycines in aqueous solutions at 18–55°C

Cited by 87 publications

References 44 publications

Calorimetric investigations of aqueous amino acid and dipeptide systems from 288. 15 to 328. 15 K

Calorimetric investigations of aqueous amino acid and dipeptide systems from 288. 15 to 328. 15 K

Urea interactions with protein groups: A volumetric study

The hydration of nucleic acid duplexes as assessed by a combination of volumetric and structural techniques

Contact Info

Product

Resources

About