Partial molar volumes and adiabatic compressibilities of unfolded protein states

Lee, So‐Young; Tikhomirova, Anna; Shalvardjian, Napol; Chalikian, Tigran V.

doi:10.1016/j.bpc.2008.02.009

Cited by 47 publications

(38 citation statements)

References 66 publications

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“…Tamura and Gekko (1995), c Kamiyama and Gekko (1997), d Gekko et al (2003), e Filfil and Chalikian (2000), f Chalikian et al (1995), g Kamiyama et al (1999), h Chalikian et al (1997) (Tamura and Gekko 1995;Kamiyama and Gekko 1997). Theseˇs o values are close to the average for unfolded proteins estimated from those of amino acid residues (Lee et al 2008). The v o values also decrease markedly in the fully unfolded states.…”

Section: Volume and Compressibility Changes Due To Conformational Tramentioning

confidence: 71%

Volume and Compressibility of Proteins

Gekko

2015

Subcellular Biochemistry

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The partial specific (or molar) volume, expansibility, and compressibility of a protein are fundamental thermodynamic quantities for characterizing its structure in solution. We review the definitions, measurements, and implications of these volumetric quantities in relation to protein structural biology. The partial specific volumes under constant molality (isomolal) and chemical potential (isopotential) conditions of the cosolvent (multicomponent systems) are explained in terms of preferential solvent interactions relevant to the solubility and stability of proteins. The partial expansibility is briefly discussed in terms of the effects of temperature on protein-solvent interactions (hydration) and internal packing defects (cavities). We discuss the compressibility-structure-function relationships of proteins based on analyses of the correlations between the partial adiabatic compressibilities and the structures or functions of various globular proteins (including mutants), focusing on the roles of the internal cavities in structural fluctuations. The volume and compressibility changes associated with various conformational transitions are also discussed in terms of the changes in hydration and cavities in order to elucidate the nonnative structures and the transition mechanisms, especially those associated with pressure denaturation.

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Section: Volume and Compressibility Changes Due To Conformational Tramentioning

confidence: 71%

Volume and Compressibility of Proteins

Gekko

2015

Subcellular Biochemistry

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“…However, K • S (R) values at T = 298.15 K for all the side-chains relevant in this study, except that for asparagine, have been reported by Sakurai, Nitta and co-workers [19,42]. More recently, Lee et al [23] have reported K • S,2 data for many N -acetyl amino acid amides. Using a relationship analogous to Eq.…”

Section: S2supporting

confidence: 53%

“…[23]. See text c Calculated using K • S (R) values derived from K • S,2 data for N -acetyl amino acid amides from Refs.…”

Section: S2mentioning

confidence: 99%

Partial Molar Isentropic Compressions of Some Tetra- and Pentapeptides in Aqueous Solution: Implications for Group Additivity Schemes for Unfolded Proteins

Hedwig

Høiland

2012

J Solution Chem

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Sound speeds have been measured for aqueous solutions of five tetrapeptides and five pentapeptides at T = 298.15 K. The partial molar isentropic compressions at infinite dilution, K • S,2 , were derived for the peptides using conventional methods. The results were compared with those calculated using group additivity methods, with the amino acid sidechain contributions derived using K • S,2 data reported previously for some tripeptides of sequence gly-X-gly, where X represents an amino acid, and also for some N -acetyl amino acid amides. The tripeptides are the preferred model compounds for the estimation of the side-chain contributions to K • S,2 of a polypeptide. Our study also confirms that simple group additivity schemes are not feasible for the estimation of K • S,2 values for polypeptides and unfolded proteins.

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“…We use partial molar volume and adiabatic compressibility data on N-acetyl amino acid amides to evaluate the pressure-dependent volumes of the 19 amino acid side chains in solution. 42 The values of V S and K S for the amino acid side chains at 25°C are presented in Table 1.…”

Section: Resultsmentioning

confidence: 99%