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Volumn 124, Issue 1, 2006, Pages 35-42

Isentropic and isothermal compressibilities of the backbone glycyl group of proteins in aqueous solution

Author keywords

Aqueous solution; Glycyl group; Partial molar isentropic compressibility; Partial molar isothermal compressibility; Peptide model compounds; Speed of sound

Indexed keywords

GLYCYLGLYCINE;

EID: 33746712115     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2006.05.002     Document Type: Article
Times cited : (16)

References (44)
  • 3
    • 0032574699 scopus 로고    scopus 로고
    • Pressure denaturation of proteins: evaluation of compressibility effects
    • Prehoda K.E., Mooberry E.S., and Markley J.L. Pressure denaturation of proteins: evaluation of compressibility effects. Biochemistry 37 (1998) 5785-5790
    • (1998) Biochemistry , vol.37 , pp. 5785-5790
    • Prehoda, K.E.1    Mooberry, E.S.2    Markley, J.L.3
  • 4
    • 0000725483 scopus 로고
    • Thermodynamic fluctuations in protein molecules
    • Cooper A. Thermodynamic fluctuations in protein molecules. Proc. Natl. Acad. Sci. U. S. A. 73 (1976) 2740-2741
    • (1976) Proc. Natl. Acad. Sci. U. S. A. , vol.73 , pp. 2740-2741
    • Cooper, A.1
  • 5
    • 20644465398 scopus 로고    scopus 로고
    • Insights into protein compressibility from molecular dynamics simulations
    • Dadarlat V.M., and Post C.B. Insights into protein compressibility from molecular dynamics simulations. J. Phys. Chem., B 105 (2001) 715-724
    • (2001) J. Phys. Chem., B , vol.105 , pp. 715-724
    • Dadarlat, V.M.1    Post, C.B.2
  • 6
    • 33845561444 scopus 로고
    • Compressibility of globular proteins in water at 25 °C
    • Gekko K., and Noguchi H. Compressibility of globular proteins in water at 25 °C. J. Phys. Chem. 83 (1979) 2706-2714
    • (1979) J. Phys. Chem. , vol.83 , pp. 2706-2714
    • Gekko, K.1    Noguchi, H.2
  • 7
    • 0008047756 scopus 로고    scopus 로고
    • The hydration of globular proteins as derived from volume and compressibility measurements: cross correlating thermodynamic and structural data
    • Chalikian T.V., Totrov M., Abagyan R., and Breslauer K.J. The hydration of globular proteins as derived from volume and compressibility measurements: cross correlating thermodynamic and structural data. J. Mol. Biol. 260 (1996) 588-603
    • (1996) J. Mol. Biol. , vol.260 , pp. 588-603
    • Chalikian, T.V.1    Totrov, M.2    Abagyan, R.3    Breslauer, K.J.4
  • 8
    • 71549133762 scopus 로고    scopus 로고
    • Hinz H.-J. (Ed), Springer, Berlin
    • Høiland H., and Hedwig G.R. In: Hinz H.-J. (Ed). Proteins Biochemical and Physical Properties. Landolt-Börnstein, New Series vol. VII/2A (2003), Springer, Berlin 6-1-6-23
    • (2003) Landolt-Börnstein, New Series , vol.VII-2A
    • Høiland, H.1    Hedwig, G.R.2
  • 9
    • 57249109776 scopus 로고    scopus 로고
    • Apparent molar isentropic compressions and expansions of solutions
    • Blandamer M.J., Davis M.I., Douhéret G., and Reis J.C.R. Apparent molar isentropic compressions and expansions of solutions. Chem. Soc. Rev. 30 (2001) 8-15
    • (2001) Chem. Soc. Rev. , vol.30 , pp. 8-15
    • Blandamer, M.J.1    Davis, M.I.2    Douhéret, G.3    Reis, J.C.R.4
  • 10
    • 0000167830 scopus 로고
    • Isothermal compressibilities of aqueous solutions of tetraalkylammonium bromides
    • Desnoyers J.E., and Philip P.R. Isothermal compressibilities of aqueous solutions of tetraalkylammonium bromides. Can. J. Chem. 50 (1972) 1094-1096
    • (1972) Can. J. Chem. , vol.50 , pp. 1094-1096
    • Desnoyers, J.E.1    Philip, P.R.2
  • 11
    • 0036498720 scopus 로고    scopus 로고
    • Determination of the volumetric properties of proteins and other solutes using pressure perturbation calorimetry
    • Lin L.-N., Brandts J.F., Brandts M.J., and Plotnikov V. Determination of the volumetric properties of proteins and other solutes using pressure perturbation calorimetry. Anal. Biochem. 302 (2002) 144-160
    • (2002) Anal. Biochem. , vol.302 , pp. 144-160
    • Lin, L.-N.1    Brandts, J.F.2    Brandts, M.J.3    Plotnikov, V.4
  • 12
    • 0036197878 scopus 로고    scopus 로고
    • Application of pressure perturbation calorimetry to lipid bilayers
    • Heerklotz H., and Seeling J. Application of pressure perturbation calorimetry to lipid bilayers. Biophys. J. 82 (2002) 1445-1452
    • (2002) Biophys. J. , vol.82 , pp. 1445-1452
    • Heerklotz, H.1    Seeling, J.2
  • 13
    • 33144483961 scopus 로고    scopus 로고
    • Pressure-modulated differential scanning calorimetry. An approach to the continuous, simultaneous determination of heat capacities and expansion coefficients
    • Bohm K., Rosgen J., and Hinz H.-J. Pressure-modulated differential scanning calorimetry. An approach to the continuous, simultaneous determination of heat capacities and expansion coefficients. Anal. Chem. 78 (2006) 984-990
    • (2006) Anal. Chem. , vol.78 , pp. 984-990
    • Bohm, K.1    Rosgen, J.2    Hinz, H.-J.3
  • 14
    • 0027993455 scopus 로고
    • Hydration and partial compressibility of biological compounds
    • Chalikian T.V., Sarvazyan A.P., and Breslauer K.J. Hydration and partial compressibility of biological compounds. Biophys. Chemist. 51 (1994) 89-109
    • (1994) Biophys. Chemist. , vol.51 , pp. 89-109
    • Chalikian, T.V.1    Sarvazyan, A.P.2    Breslauer, K.J.3
  • 15
    • 0022999267 scopus 로고
    • Compressibility-structure relationship of globular proteins
    • Gekko K., and Hasegawa Y. Compressibility-structure relationship of globular proteins. Biochemistry 25 (1986) 6563-6571
    • (1986) Biochemistry , vol.25 , pp. 6563-6571
    • Gekko, K.1    Hasegawa, Y.2
  • 16
    • 0035815110 scopus 로고    scopus 로고
    • Volume, expansivity and isothermal compressibility changes associated with temperature and pressure unfolding of staphylococcal nuclease
    • Seemann H., Winter R., and Royer C.A. Volume, expansivity and isothermal compressibility changes associated with temperature and pressure unfolding of staphylococcal nuclease. J. Mol. Biol. 307 (2001) 1091-1102
    • (2001) J. Mol. Biol. , vol.307 , pp. 1091-1102
    • Seemann, H.1    Winter, R.2    Royer, C.A.3
  • 17
    • 0030034601 scopus 로고    scopus 로고
    • Compressibility as a means to detect and characterize globular protein states
    • Chalikian T.V., and Breslauer K.J. Compressibility as a means to detect and characterize globular protein states. Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 1012-1014
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 1012-1014
    • Chalikian, T.V.1    Breslauer, K.J.2
  • 19
    • 3843104610 scopus 로고    scopus 로고
    • Partial molar isentropic and isothermal compressibilities of some N-acetyl amino acid amides in aqueous solution at 298.15 K
    • Hedwig G.R., and Høiland H. Partial molar isentropic and isothermal compressibilities of some N-acetyl amino acid amides in aqueous solution at 298.15 K. Phys. Chem. Chem. Phys. 6 (2004) 2440-2445
    • (2004) Phys. Chem. Chem. Phys. , vol.6 , pp. 2440-2445
    • Hedwig, G.R.1    Høiland, H.2
  • 21
    • 0031490948 scopus 로고    scopus 로고
    • Partial molar volumes and adiabatic compressibilities of N-acetyl-dl-serinamide and N-acetyl-l-threoninamide in dilute aqueous solution
    • Mizuguchi M., Sakurai M., and Nitta K. Partial molar volumes and adiabatic compressibilities of N-acetyl-dl-serinamide and N-acetyl-l-threoninamide in dilute aqueous solution. J. Solution Chem. 26 (1997) 579-594
    • (1997) J. Solution Chem. , vol.26 , pp. 579-594
    • Mizuguchi, M.1    Sakurai, M.2    Nitta, K.3
  • 22
    • 0030787855 scopus 로고    scopus 로고
    • Partial molar volumes and compressibilities of extended polypeptide chains in aqueous solution: additivity scheme and implication of protein unfolding at normal and high pressure
    • Kharakoz D.P. Partial molar volumes and compressibilities of extended polypeptide chains in aqueous solution: additivity scheme and implication of protein unfolding at normal and high pressure. Biochemistry 36 (1997) 10276-10285
    • (1997) Biochemistry , vol.36 , pp. 10276-10285
    • Kharakoz, D.P.1
  • 23
    • 0001426227 scopus 로고
    • Partial molar volumes and adiabatic compressibilities of amino acids in dilute aqueous solutions at 5, 15, 25, 35, and 45 °C
    • Kikuchi M., Sakurai M., and Nitta K. Partial molar volumes and adiabatic compressibilities of amino acids in dilute aqueous solutions at 5, 15, 25, 35, and 45 °C. J. Chem. Eng. Data 40 (1995) 935-942
    • (1995) J. Chem. Eng. Data , vol.40 , pp. 935-942
    • Kikuchi, M.1    Sakurai, M.2    Nitta, K.3
  • 24
    • 0028413422 scopus 로고
    • Partial molar volumes, expansibilities, and compressibilities of oligoglycines in aqueous solutions at 18-55 °C
    • Chalikian T.V., Sarvazyan A.P., Funck T., and Breslauer K.J. Partial molar volumes, expansibilities, and compressibilities of oligoglycines in aqueous solutions at 18-55 °C. Biopolymers 34 (1994) 541-553
    • (1994) Biopolymers , vol.34 , pp. 541-553
    • Chalikian, T.V.1    Sarvazyan, A.P.2    Funck, T.3    Breslauer, K.J.4
  • 25
    • 33746694701 scopus 로고    scopus 로고
    • N.M. Wise, G.R. Hedwig, The partial molar volume and heat capacity of the glycyl group in aqueous solution at 25 °C, J. Solution Chem. 35 (in press).
  • 26
    • 0001501863 scopus 로고
    • Thermodynamic properties of peptide solutions: Part 6. The amino acid side-chain contributions to the partial molar volumes and heat capacities of some tripeptides in aqueous solution
    • Reading J.F., and Hedwig G.R. Thermodynamic properties of peptide solutions: Part 6. The amino acid side-chain contributions to the partial molar volumes and heat capacities of some tripeptides in aqueous solution. J. Chem. Soc., Faraday Trans. 86 (1990) 3117-3123
    • (1990) J. Chem. Soc., Faraday Trans. , vol.86 , pp. 3117-3123
    • Reading, J.F.1    Hedwig, G.R.2
  • 27
    • 34250090518 scopus 로고
    • Thermodynamic properties of peptide solutions: 3. Partial molar volumes and partial molar heat capacities of some tripeptides in aqueous solution
    • Hedwig G.R. Thermodynamic properties of peptide solutions: 3. Partial molar volumes and partial molar heat capacities of some tripeptides in aqueous solution. J. Solution Chem. 17 (1988) 383-397
    • (1988) J. Solution Chem. , vol.17 , pp. 383-397
    • Hedwig, G.R.1
  • 29
    • 0000493061 scopus 로고
    • An automated apparatus for ultrasound velocity measurements improving the pulse-echo-overlap method to a precision better than 0.5 ppm in liquids
    • Horvat-Szabo G., Høgseth E., and Høiland H. An automated apparatus for ultrasound velocity measurements improving the pulse-echo-overlap method to a precision better than 0.5 ppm in liquids. Rev. Sci. Instrum. 65 (1994) 1644-1648
    • (1994) Rev. Sci. Instrum. , vol.65 , pp. 1644-1648
    • Horvat-Szabo, G.1    Høgseth, E.2    Høiland, H.3
  • 30
    • 0009979659 scopus 로고
    • Precise representation of volume properties of water at one atmosphere
    • Kell G.S. Precise representation of volume properties of water at one atmosphere. J. Chem. Eng. Data 12 (1967) 66-69
    • (1967) J. Chem. Eng. Data , vol.12 , pp. 66-69
    • Kell, G.S.1
  • 31
    • 0037605067 scopus 로고    scopus 로고
    • Partial molar volumes of proteins: amino acid side-chain contributions derived from the partial molar volumes of some tripeptides over the temperature range 10-90 °C
    • Häckel M., Hinz H.-J., and Hedwig G.R. Partial molar volumes of proteins: amino acid side-chain contributions derived from the partial molar volumes of some tripeptides over the temperature range 10-90 °C. Biophys. Chemist. 82 (1999) 35-50
    • (1999) Biophys. Chemist. , vol.82 , pp. 35-50
    • Häckel, M.1    Hinz, H.-J.2    Hedwig, G.R.3
  • 32
    • 0034327382 scopus 로고    scopus 로고
    • The partial molar volumes of some tetra- and pentapeptides in aqueous solution: a test of amino acid side-chain group additivity for unfolded proteins
    • Häckel M., Hinz H.-J., and Hedwig G.R. The partial molar volumes of some tetra- and pentapeptides in aqueous solution: a test of amino acid side-chain group additivity for unfolded proteins. Phys. Chem. Chem. Phys. 2 (2000) 4843-4849
    • (2000) Phys. Chem. Chem. Phys. , vol.2 , pp. 4843-4849
    • Häckel, M.1    Hinz, H.-J.2    Hedwig, G.R.3
  • 34
    • 0028369444 scopus 로고
    • Apparent molar heat capacities and volumes of some aqueous solutions of aliphatic amino acids at 288.15, 2981.5, 313.15, and 328.15 K
    • Hakin A.W., Duke M.M., Klassen S.A., McKay R.M., and Preuss K.E. Apparent molar heat capacities and volumes of some aqueous solutions of aliphatic amino acids at 288.15, 2981.5, 313.15, and 328.15 K. Can. J. Chem. 72 (1994) 362-368
    • (1994) Can. J. Chem. , vol.72 , pp. 362-368
    • Hakin, A.W.1    Duke, M.M.2    Klassen, S.A.3    McKay, R.M.4    Preuss, K.E.5
  • 38
    • 34249928742 scopus 로고
    • Thermodynamic properties of peptide solutions: 7. Partial molar isentropic pressure coefficients of some dipeptides in aqueous solution
    • Hedwig G.R., and Høiland H. Thermodynamic properties of peptide solutions: 7. Partial molar isentropic pressure coefficients of some dipeptides in aqueous solution. J. Solution Chem. 20 (1991) 1113-1127
    • (1991) J. Solution Chem. , vol.20 , pp. 1113-1127
    • Hedwig, G.R.1    Høiland, H.2
  • 39
    • 84915609421 scopus 로고
    • Heat units and temperature scales for calorimetry
    • Stimson H.F. Heat units and temperature scales for calorimetry. Am. J. Phys. 23 (1955) 614-622
    • (1955) Am. J. Phys. , vol.23 , pp. 614-622
    • Stimson, H.F.1
  • 40
    • 0344103144 scopus 로고
    • Density, thermal expansivity, and compressibitity of liquid water from 0 °C to 150 °C: correlations and tables for atmospheric pressure and saturation reviewed and expressed on 1968 temperature scale
    • Kell G.S. Density, thermal expansivity, and compressibitity of liquid water from 0 °C to 150 °C: correlations and tables for atmospheric pressure and saturation reviewed and expressed on 1968 temperature scale. J. Chem. Eng. Data 20 (1975) 97-105
    • (1975) J. Chem. Eng. Data , vol.20 , pp. 97-105
    • Kell, G.S.1
  • 41
    • 51649185351 scopus 로고
    • Partial molal compressibilities of salts in aqueous solution and assignment of ionic contributions
    • Mathieson J.G., and Conway B.E. Partial molal compressibilities of salts in aqueous solution and assignment of ionic contributions. J. Solution Chem. 3 (1974) 455-477
    • (1974) J. Solution Chem. , vol.3 , pp. 455-477
    • Mathieson, J.G.1    Conway, B.E.2
  • 42
    • 0021392451 scopus 로고
    • Volume and adiabatic compressibility of amino acids in urea-water mixtures
    • Ogawa T., Yasuda M., and Mizutani K. Volume and adiabatic compressibility of amino acids in urea-water mixtures. Bull. Chem. Soc. Jpn. 57 (1984) 662-666
    • (1984) Bull. Chem. Soc. Jpn. , vol.57 , pp. 662-666
    • Ogawa, T.1    Yasuda, M.2    Mizutani, K.3
  • 43
    • 0001514917 scopus 로고
    • Partial molar volumes, expansibilities, and compressibilities of α,ω-aminocarboxylic acids in aqueous solution between 18 and 55 °C
    • Chalikian T.V., Sarvazyan A.P., and Breslauer K.J. Partial molar volumes, expansibilities, and compressibilities of α,ω-aminocarboxylic acids in aqueous solution between 18 and 55 °C. J. Phys. Chem. 97 (1993) 13017-13026
    • (1993) J. Phys. Chem. , vol.97 , pp. 13017-13026
    • Chalikian, T.V.1    Sarvazyan, A.P.2    Breslauer, K.J.3
  • 44
    • 33751499294 scopus 로고
    • Volumetric properties of proteins and their analogues in diluted water solutions: 2. Partial adiabatic compressibilities of amino acids at 15-70 °C
    • Kharakoz D.P. Volumetric properties of proteins and their analogues in diluted water solutions: 2. Partial adiabatic compressibilities of amino acids at 15-70 °C. J. Phys. Chem. 95 (1991) 5634-5642
    • (1991) J. Phys. Chem. , vol.95 , pp. 5634-5642
    • Kharakoz, D.P.1


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