A new set of peptide-based group heat capacities for use in protein stability calculations

Häckel, Marko; Hinz, Hans‐Jürgen; Hedwig, Gavin R.

doi:10.1006/jmbi.1999.2952

Cited by 74 publications

(68 citation statements)

References 59 publications

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“…The latter values were calculated from the standard molal Gibbs energies and enthalpies of ionization ( G • ion and H • ion ) of these charged species taken from Goldberg et al ( ) Kikuchi et al, 1995;( ) Kharakoz, 1991; ( ) Mizuguchi et al, 1997;( ) Yasuda et al, 1998;and (×) Millero et al, 1978. ( ) Vogl et al (1995); ( ) Häckel et al (1998); (♦) Häckel et al (1999a); ( ) Downes and Hedwig, 1995;( ) ( ) Vogl et al (1995); ( ) Häckel et al (1998); (♦) Häckel et al (1999b). www.biogeosciences.net/bg/0000/0001/ Biogeosciences, 0000, 0001-26, 2006 together with the properties of the corresponding neutral species given in Table 2.…”

Section: Groupmentioning

confidence: 99%

“…The polynomial equations representing the experimental measurements of C • P and V • of the Gly-X-Gly tripeptides given by Vogl et al (1995), Häckel et al (1998), andHäckel et al (1999a) were used to generate the values at 15, 25, 40, 55, 70, 80, 90, and 100 • C shown in Figs. 2d and e.…”

Section: Retrieval Of Non-solvation Parametersmentioning

confidence: 99%

“…where E • represents the standard molal isobaric expansibility of the amino acid, and C : Häckel et al (1999a).…”

Section: Retrieval Of Non-solvation Parametersmentioning

confidence: 99%

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Temperature, pressure, and electrochemical constraints on protein speciation: Group additivity calculation of the standard molal thermodynamic properties of ionized unfolded proteins

2006

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Abstract. Thermodynamic calculations can be used to quantify environmental constraints on the speciation of proteins, such as the pH and temperature dependence of ionization state, and the relative chemical stabilities of proteins in different biogeochemical settings. These calculations depend in part on values of the standard molal Gibbs energies of proteins and their ionization reactions as a function of temperature and pressure. Because these values are not generally available, we calculated values of the standard molal thermodynamic properties at 25 • C and 1 bar as well as the revised Helgeson-Kirkham-Flowers equations of state parameters of neutral and charged zwitterionic reference model compounds including aqueous amino acids, polypeptides, and unfolded proteins. The experimental calorimetric and volumetric data for these species taken from the literature were combined with group additivity algorithms to calculate the properties and parameters of neutral and ionized sidechain and backbone groups in unfolded proteins. The resulting set of group contributions enables the calculation of the standard molal Gibbs energy, enthalpy, entropy, isobaric heat capacity, volume, and isothermal compressibility of unfolded proteins in a range of proton ionization states to temperatures and pressures exceeding 100 • C and 1000 bar. This approach provides a useful frame of reference for thermodynamic studies of protein folding and complexation reactions. It can also be used to assign provisional values of the net charge and Gibbs energy of ionized proteins as a function of temperature and pH. Using these values, an Eh-pH diagram for a reaction representing the speciation of extracellular proteins from Pyrococcus furiosus and Bacillus subtilis was generated. The predicted predominance limits of these proteins correspond with the different electrochemical conditions of hydrothermal vents and soils. More comprehensive calculations of this kind may reveal pervasive chemical potential constraints on the interactions of microbes with their environment.

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Section: Groupmentioning

confidence: 99%

Section: Retrieval Of Non-solvation Parametersmentioning

confidence: 99%

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Temperature, pressure, and electrochemical constraints on protein speciation: Group additivity calculation of the standard molal thermodynamic properties of ionized unfolded proteins

2006

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“…(5,(7)(8)(9) One of the advantages of using additivity schemes to derive the thermodynamic properties of aqueous protein systems is the possibility of being able to estimate their properties under extreme conditions of temperature and pressure. (7) This strategy is used because the direct determinations of the thermodynamic properties of such species are often beset by many experimental difficulties.…”

Section: Introductionmentioning

confidence: 99%

“…Most notably, the thermodynamic properties of such species under extreme conditions can be used to probe questions surrounding the origins of life in deep-sea hydrothermal vent habitats. (11)(12)(13) Although most studies of the thermodynamic properties of biological model compounds have been conducted at temperatures and pressures close to ambient, the apparent molar heat capacities of some model compounds in aqueous solution have been determined at temperatures up to 373.15 K (5) and 398.15 K (8) using commercial differential scanning calorimeters. However, to explore the high-temperature and -pressure surfaces of any thermodynamic property of interest, researchers have to use highly specialized noncommercial instrumentation.…”

Section: Introductionmentioning

confidence: 99%

The partial molar heat capacities of glycine and glycylglycine in aqueous solution at elevated temperatures and atp= 10.0 MPa

Downes¹,

Hakin

Hedwig

2001

The Journal of Chemical Thermodynamics

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Conformational Behavior of Intrinsically Disordered Proteins: Effects of Strong Denaturants, Temperature, PH, Counterions, and Macromolecular Crowding

Uversky

2010

Instrumental Analysis of Intrinsically Disordered Proteins

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19Intrinsically disordered proteins (IDPs) differ from " normal " ordered proteins at several levels: structural, functional, and conformational. Amino acid biases characteristic for IDPs (e.g., low content of hydrophobic amino acid residues combined with high relative content of charged and polar residues) determine their structural variability and lack of rigid well -folded structure. This structural plasticity is necessary for the unique functional repertoire of IDPs, which is complementary to the catalytic activities of ordered proteins. Amino acid biases also drive atypical responses of IDPs to changes in their environment. The conformational behavior of IDPs is characterized by the ABSTRACT

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A new set of peptide-based group heat capacities for use in protein stability calculations

Cited by 74 publications

References 59 publications

Temperature, pressure, and electrochemical constraints on protein speciation: Group additivity calculation of the standard molal thermodynamic properties of ionized unfolded proteins

Temperature, pressure, and electrochemical constraints on protein speciation: Group additivity calculation of the standard molal thermodynamic properties of ionized unfolded proteins

The partial molar heat capacities of glycine and glycylglycine in aqueous solution at elevated temperatures and atp= 10.0 MPa

Conformational Behavior of Intrinsically Disordered Proteins: Effects of Strong Denaturants, Temperature, PH, Counterions, and Macromolecular Crowding

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