메뉴 건너뛰기




Volumn 9, Issue 7, 2000, Pages 1340-1346

The unfolding enthalpy of the pH 4 molten globule of apomyoglobin measured by isothermal titration calorimetry

Author keywords

Apomyoglobin; Molten globule; Titration calorimetry; Unfolding enthalpy

Indexed keywords

APOMYOGLOBIN;

EID: 0033864682     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.9.7.1340     Document Type: Article
Times cited : (35)

References (39)
  • 2
    • 0000180763 scopus 로고
    • Temperature dependence of the hydrophobic interaction in protein folding
    • Baldwin RL. 1986. Temperature dependence of the hydrophobic interaction in protein folding. Proc Natl Acad Sci USA 83:8069-8072.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 8069-8072
    • Baldwin, R.L.1
  • 3
    • 6244250502 scopus 로고
    • The role of hydrogen bonds in protein folding and protein association
    • Ben-Naim A. 1991. The role of hydrogen bonds in protein folding and protein association. J Phys Chem 95:1437-1444.
    • (1991) J Phys Chem , vol.95 , pp. 1437-1444
    • Ben-Naim, A.1
  • 5
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • Edelhoch H. 1967. Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry 6:1948-1954.
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 7
    • 0031932824 scopus 로고    scopus 로고
    • Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding
    • Eliezer D, Yao J, Dyson HD, Wright PE. 1998. Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding. Nat Struct Biol 5:148-155.
    • (1998) Nat Struct Biol , vol.5 , pp. 148-155
    • Eliezer, D.1    Yao, J.2    Dyson, H.D.3    Wright, P.E.4
  • 8
    • 0001022707 scopus 로고    scopus 로고
    • Protonation behavior of histidine 24 and histidine 119 in forming the pH 4 folding intermediate of apomyoglobin
    • Geierstanger B, Jamin M, Volkman BF, Baldwin RL. 1998. Protonation behavior of histidine 24 and histidine 119 in forming the pH 4 folding intermediate of apomyoglobin. Biochemistry 37:4254-4265.
    • (1998) Biochemistry , vol.37 , pp. 4254-4265
    • Geierstanger, B.1    Jamin, M.2    Volkman, B.F.3    Baldwin, R.L.4
  • 9
    • 3042788225 scopus 로고
    • Calorimetric determination of enthalpies of solution of slightly soluble liquids. II. Enthalpy of solution of some hydrocarbons in water and their use in establishing the temperature dependence of their solubilities
    • Gill SJ, Nichols NF, Wadso I. 1976. Calorimetric determination of enthalpies of solution of slightly soluble liquids. II. Enthalpy of solution of some hydrocarbons in water and their use in establishing the temperature dependence of their solubilities. J Chem Thermodyn 8:445-452.
    • (1976) J Chem Thermodyn , vol.8 , pp. 445-452
    • Gill, S.J.1    Nichols, N.F.2    Wadso, I.3
  • 10
    • 0028174361 scopus 로고
    • Energetics of the α-lactalbumin states: A calorimetric and statistical thermodynamic study
    • Griko YuV, Freire E, Privalov PL. 1994. Energetics of the α-lactalbumin states: A calorimetric and statistical thermodynamic study. Biochemistry 33:1889-1899.
    • (1994) Biochemistry , vol.33 , pp. 1889-1899
    • Griko, Yu.V.1    Freire, E.2    Privalov, P.L.3
  • 11
    • 0028329347 scopus 로고
    • Thermodynamic puzzle of apomyoglobin unfolding
    • Griko YuV, Privalov PL. 1994. Thermodynamic puzzle of apomyoglobin unfolding. J Mol Biol 235:1318-1325.
    • (1994) J Mol Biol , vol.235 , pp. 1318-1325
    • Griko, Yu.V.1    Privalov, P.L.2
  • 13
    • 0001220959 scopus 로고
    • Salt-induced formation of the molten globule state of apomyoglobin studied by isothermal titration calorimetry
    • Hamada D, Fukada H, Takahashi K, Goto Y. 1995. Salt-induced formation of the molten globule state of apomyoglobin studied by isothermal titration calorimetry. Thermochim Acta 266:385-400.
    • (1995) Thermochim Acta , vol.266 , pp. 385-400
    • Hamada, D.1    Fukada, H.2    Takahashi, K.3    Goto, Y.4
  • 14
    • 0028143596 scopus 로고
    • Salt-induced formation of the molten globule state of cytochrome c studied by isothermal titration calorimetry
    • Hamada D, Kidokoro S, Fukada H, Takahashi K, Goto Y. 1994. Salt-induced formation of the molten globule state of cytochrome c studied by isothermal titration calorimetry. Proc Natl Acad Sci USA 91:10325-10329.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 10325-10329
    • Hamada, D.1    Kidokoro, S.2    Fukada, H.3    Takahashi, K.4    Goto, Y.5
  • 15
    • 0027422525 scopus 로고
    • Covalent bond changes as a driving force in enzyme catalysis
    • Huang Y, Bolen DW. 1993. Covalent bond changes as a driving force in enzyme catalysis. Biochemistry 32:9329-9339.
    • (1993) Biochemistry , vol.32 , pp. 9329-9339
    • Huang, Y.1    Bolen, D.W.2
  • 16
    • 0025186451 scopus 로고
    • Structural characterization of a partly folded apomyoglobin intermediate
    • Hughson FM, Wright PE, Baldwin RL. 1990. Structural characterization of a partly folded apomyoglobin intermediate. Science 249:1544-1548.
    • (1990) Science , vol.249 , pp. 1544-1548
    • Hughson, F.M.1    Wright, P.E.2    Baldwin, R.L.3
  • 17
    • 0029904282 scopus 로고    scopus 로고
    • Refolding and unfolding kinetics of the equilibrium folding intermediate of apomyoglobin
    • Jamin M, Baldwin RL. 1996. Refolding and unfolding kinetics of the equilibrium folding intermediate of apomyoglobin. Nat Struct Biol 3:613-618.
    • (1996) Nat Struct Biol , vol.3 , pp. 613-618
    • Jamin, M.1    Baldwin, R.L.2
  • 18
    • 0032549072 scopus 로고    scopus 로고
    • Two forms of the pH 4 folding intermediate of apomyoglobin
    • Jamin M, Baldwin RL. 1998. Two forms of the pH 4 folding intermediate of apomyoglobin. J Mol Biol 276:491-504.
    • (1998) J Mol Biol , vol.276 , pp. 491-504
    • Jamin, M.1    Baldwin, R.L.2
  • 19
    • 0033600716 scopus 로고    scopus 로고
    • Submillisecond unfolding kinetics of apomyoglobin and its pH 4 intermediate
    • Jamin M, Yen S-R, Rousseau DL, Baldwin RL. 1999. Submillisecond unfolding kinetics of apomyoglobin and its pH 4 intermediate. J Mol Biol 292:731-740.
    • (1999) J Mol Biol , vol.292 , pp. 731-740
    • Jamin, M.1    Yen, S.-R.2    Rousseau, D.L.3    Baldwin, R.L.4
  • 20
    • 0029981924 scopus 로고    scopus 로고
    • Packing interactions in the apomyoglobin folding intermediate
    • Kay MS, Baldwin RL. 1996. Packing interactions in the apomyoglobin folding intermediate. Nat Struct Biol 3:439-445.
    • (1996) Nat Struct Biol , vol.3 , pp. 439-445
    • Kay, M.S.1    Baldwin, R.L.2
  • 21
    • 0032568639 scopus 로고    scopus 로고
    • Alternative models for describing the acid unfolding of the apomyoglobin folding intermediate
    • Kay MS, Baldwin RL. 1998. Alternative models for describing the acid unfolding of the apomyoglobin folding intermediate. Biochemistry 37:7859-7868.
    • (1998) Biochemistry , vol.37 , pp. 7859-7868
    • Kay, M.S.1    Baldwin, R.L.2
  • 22
    • 0033514920 scopus 로고    scopus 로고
    • Specificity of native-like interhelical Hydrophobic contacts in the apomyoglobin intermediate
    • Kay MS, Ramos CHI, Baldwin RL. 1999. Specificity of native-like interhelical Hydrophobic contacts in the apomyoglobin intermediate. Proc Natl Acad Sci USA 96:2007-2012.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 2007-2012
    • Kay, M.S.1    Ramos, C.H.I.2    Baldwin, R.L.3
  • 23
    • 0015237085 scopus 로고
    • On the nature of the protein interior
    • Klapper MH. 1971. On the nature of the protein interior. Biochim Biophys Acta 229:557-566.
    • (1971) Biochim Biophys Acta , vol.229 , pp. 557-566
    • Klapper, M.H.1
  • 24
    • 0029014386 scopus 로고
    • Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway
    • Loh SN, Kay MS, Baldwin RL. 1995. Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway. Proc Natl Acad Sci USA 92:5446-5450.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 5446-5450
    • Loh, S.N.1    Kay, M.S.2    Baldwin, R.L.3
  • 25
    • 0033613115 scopus 로고    scopus 로고
    • The 28-111 disulfide bond constrains the a-lactalbumin molten globule and weakens its cooperativity of folding
    • Luo Y, Baldwin RL. 1999. The 28-111 disulfide bond constrains the a-lactalbumin molten globule and weakens its cooperativity of folding. Proc Natl Acad Sci USA 96:11283-11287.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 11283-11287
    • Luo, Y.1    Baldwin, R.L.2
  • 26
    • 0030694241 scopus 로고    scopus 로고
    • Cooperativity of folding of the apomyoglobin pH 4 intermediate studied by glycine and proline mutations
    • Luo Y, Kay MS, Baldwin RL. 1997. Cooperativity of folding of the apomyoglobin pH 4 intermediate studied by glycine and proline mutations. Nat Struct Biol 4:925-930.
    • (1997) Nat Struct Biol , vol.4 , pp. 925-930
    • Luo, Y.1    Kay, M.S.2    Baldwin, R.L.3
  • 27
    • 0027305948 scopus 로고
    • Contribution of hydration to protein folding thermodynamics, 1. The enthalpy of hydration
    • Makhaladze GI, Privalov PL. 1993. Contribution of hydration to protein folding thermodynamics, 1. The enthalpy of hydration. J Mol Biol 232:639-659.
    • (1993) J Mol Biol , vol.232 , pp. 639-659
    • Makhaladze, G.I.1    Privalov, P.L.2
  • 28
    • 0029040449 scopus 로고
    • Thermodynamic stability of the molten globule states of apomyoglobin
    • Nishii I, Kataoka M, Goto Y. 1995. Thermodynamic stability of the molten globule states of apomyoglobin. J Mol Biol 250:223-238.
    • (1995) J Mol Biol , vol.250 , pp. 223-238
    • Nishii, I.1    Kataoka, M.2    Goto, Y.3
  • 29
    • 0017429069 scopus 로고
    • Areas, volumes, packing, and protein structure
    • Richards FM. 1977. Areas, volumes, packing, and protein structure. Ann Rev Biophys Bioeng 6:151-176.
    • (1977) Ann Rev Biophys Bioeng , vol.6 , pp. 151-176
    • Richards, F.M.1
  • 30
    • 0033613218 scopus 로고    scopus 로고
    • MEARA sequence of human CstF-64 polyadenylation factor is helical in solution. Aspectroscopic and calorimetric study
    • Richardson JM, McMahon KW, MacDonald CC, Makhatadze GI. 1999. MEARA sequence of human CstF-64 polyadenylation factor is helical in solution. Aspectroscopic and calorimetric study. Biochemistry 39:12869-12875.
    • (1999) Biochemistry , vol.39 , pp. 12869-12875
    • Richardson, J.M.1    McMahon, K.W.2    MacDonald, C.C.3    Makhatadze, G.I.4
  • 31
    • 49749194276 scopus 로고
    • Studies on the structure of hemoglobin. 1. Physicochemical properties of human globin
    • Rossi-Fanelli A, Antonini E, Caputo A. 1958. Studies on the structure of hemoglobin. 1. Physicochemical properties of human globin. Biochim Biophys Acta 30:608-615.
    • (1958) Biochim Biophys Acta , vol.30 , pp. 608-615
    • Rossi-Fanelli, A.1    Antonini, E.2    Caputo, A.3
  • 32
    • 33947483983 scopus 로고
    • Potentiometric titrations using Gran plots
    • Rossotti FJC, Rossotti H. 1965. Potentiometric titrations using Gran plots. J Chem Ed 42:375-378.
    • (1965) J Chem Ed , vol.42 , pp. 375-378
    • Rossotti, F.J.C.1    Rossotti, H.2
  • 33
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants
    • Santoro MM, Bolen DW. 1988, Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants. Biochemistry 27:8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 35
    • 0005123886 scopus 로고
    • Thermodynamic properties of solutions of amino acids and related substances. VIII. The ionization of glycylglycine, ∈-aminocaproic acid, and aspartic acid in aqueous solution from one to fifty degrees
    • Smith ERB, Smith PK. 1942. Thermodynamic properties of solutions of amino acids and related substances. VIII. The ionization of glycylglycine, ∈-aminocaproic acid, and aspartic acid in aqueous solution from one to fifty degrees. J Biol Chem 146:187-195.
    • (1942) J Biol Chem , vol.146 , pp. 187-195
    • Smith, E.R.B.1    Smith, P.K.2
  • 36
    • 0033609809 scopus 로고    scopus 로고
    • A calorimetric study of an α-helix with covalently closed N and C-terminal loops
    • Taylor JW, Greenfield NJ, Wu B, Privalov PL. 1999. A calorimetric study of an α-helix with covalently closed N and C-terminal loops. J Mol Biol 291:965-476.
    • (1999) J Mol Biol , vol.291 , pp. 965-1476
    • Taylor, J.W.1    Greenfield, N.J.2    Wu, B.3    Privalov, P.L.4
  • 37
    • 0026800672 scopus 로고
    • Analysis of the heat capacity dependence of protein folding
    • Yang A-S, Sharp KA, Honig B. 1992. Analysis of the heat capacity dependence of protein folding. J Mol Biol 227:889-900.
    • (1992) J Mol Biol , vol.227 , pp. 889-900
    • Yang, A.-S.1    Sharp, K.A.2    Honig, B.3
  • 38
    • 0028960492 scopus 로고
    • How valid are denaturant-induced unfolding free energy measurements? Level of conformance to common assumptions over an extended range of ribonuclease A stability
    • Yao M, Bolen DW. 1995. How valid are denaturant-induced unfolding free energy measurements? Level of conformance to common assumptions over an extended range of ribonuclease A stability. Biochemistry 34:3771-3781.
    • (1995) Biochemistry , vol.34 , pp. 3771-3781
    • Yao, M.1    Bolen, D.W.2
  • 39
    • 0026679847 scopus 로고
    • Absence of the thermal transition in apo-α-lactalbumin in the molten globule state. A study by differential scanning calorimetry
    • Yutani K, Ogasahara K, Kuwajima K. 1992. Absence of the thermal transition in apo-α-lactalbumin in the molten globule state. A study by differential scanning calorimetry. J Mol Biol 228:347-350.
    • (1992) J Mol Biol , vol.228 , pp. 347-350
    • Yutani, K.1    Ogasahara, K.2    Kuwajima, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.