메뉴 건너뛰기




Volumn 277, Issue 2, 1998, Pages 409-418

The conformational equilibrium of human growth hormone

Author keywords

Calorimetry; Folding intermediates; Human growth hormone; Protein stability; Thermodynamics

Indexed keywords

HISTIDINE; HUMAN GROWTH HORMONE; TYROSINE;

EID: 0032571246     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1613     Document Type: Article
Times cited : (34)

References (32)
  • 1
    • 0026707376 scopus 로고
    • Characterization of tertiary interactions in a folded protein by NMR methods: Studies of pH-induced structural changes in human growth hormone
    • Abildgaard F., Jorgensen A.M.M., Led J.J., Christensen T., Jensen E.B., Junker F., Dalboge H. Characterization of tertiary interactions in a folded protein by NMR methods studies of pH-induced structural changes in human growth hormone. Biochemistry. 31:1992;8587-8596
    • (1992) Biochemistry , vol.31 , pp. 8587-8596
    • Abildgaard, F.1    Jorgensen, A.M.M.2    Led, J.J.3    Christensen, T.4    Jensen, E.B.5    Junker, F.6    Dalboge, H.7
  • 2
    • 0024560535 scopus 로고
    • Folding of bovine growth hormone is consistent with the molten globule hypothesis
    • Brems D.N., Havel H.A. Folding of bovine growth hormone is consistent with the molten globule hypothesis. Proteins: Struct. Funct. Genet. 5:1989;93-95
    • (1989) Proteins: Struct. Funct. Genet. , vol.5 , pp. 93-95
    • Brems, D.N.1    Havel, H.A.2
  • 3
    • 0343247668 scopus 로고    scopus 로고
    • The native and heat-induced denatured states of alpha-chymotrypsinogen A: Thermodynamic and spectroscopic studies
    • Chalikian T.V., Volker J., Anafi D., Breslauer K.D. The native and heat-induced denatured states of alpha-chymotrypsinogen A thermodynamic and spectroscopic studies. J. Mol. Biol. 274:1997;237-252
    • (1997) J. Mol. Biol. , vol.274 , pp. 237-252
    • Chalikian, T.V.1    Volker, J.2    Anafi, D.3    Breslauer, K.D.4
  • 4
    • 0029746061 scopus 로고    scopus 로고
    • Detection of rare partially folded molecules in equilibrium with the native conformation of RnaseH
    • Chamberlain A.K., Handel T.M., Marqusee S. Detection of rare partially folded molecules in equilibrium with the native conformation of RnaseH. Nature Struct. Biol. 3:1996;782-787
    • (1996) Nature Struct. Biol. , vol.3 , pp. 782-787
    • Chamberlain, A.K.1    Handel, T.M.2    Marqusee, S.3
  • 5
    • 0027502115 scopus 로고
    • Evidence for a self-associating equilibrium intermediate during folding of human growth hormone
    • DeFelippis M.R., Alter L.A., Pekar A.H., Havel H.A., Brems D.N. Evidence for a self-associating equilibrium intermediate during folding of human growth hormone. Biochemistry. 32:1993;1555-1562
    • (1993) Biochemistry , vol.32 , pp. 1555-1562
    • Defelippis, M.R.1    Alter, L.A.2    Pekar, A.H.3    Havel, H.A.4    Brems, D.N.5
  • 7
    • 0000103534 scopus 로고
    • Statistical thermodynamic analysis of the heat capacity function associated with protein folding-unfolding transitions
    • Freire E. Statistical thermodynamic analysis of the heat capacity function associated with protein folding-unfolding transitions. Comments Mol. Cell. Biophys. 6:(2):1989;123-140
    • (1989) Comments Mol. Cell. Biophys. , vol.6 , Issue.2 , pp. 123-140
    • Freire, E.1
  • 8
    • 0029132790 scopus 로고
    • Thermodynamics of partly folded intermediates in proteins
    • Freire E. Thermodynamics of partly folded intermediates in proteins. Annu. Rev. Biophys. Biomol. Struct. 24:1995;141-165
    • (1995) Annu. Rev. Biophys. Biomol. Struct. , vol.24 , pp. 141-165
    • Freire, E.1
  • 9
    • 85030333895 scopus 로고    scopus 로고
    • The statistical thermodynamic linkage between conformational and binding equilibrium
    • In the press
    • Freire E. The statistical thermodynamic linkage between conformational and binding equilibrium. Advan. Protein Chem. 1997;. In the press
    • (1997) Advan. Protein Chem.
    • Freire, E.1
  • 10
    • 0027424690 scopus 로고
    • Molecular basis of cooperativity in protein folding. IV. CORE: A general cooperative folding model
    • Freire E., Haynie D.T., Xie D. Molecular basis of cooperativity in protein folding. IV. CORE a general cooperative folding model. Proteins: Struct. Funct. Genet. 17:1993;111-123
    • (1993) Proteins: Struct. Funct. Genet. , vol.17 , pp. 111-123
    • Freire, E.1    Haynie, D.T.2    Xie, D.3
  • 14
    • 0026351184 scopus 로고
    • Role of electrostatic repulsion in the acidic molten globule of cytochrome c
    • Goto Y., Nishikiori S. Role of electrostatic repulsion in the acidic molten globule of cytochrome c. J. Mol. Biol. 222:1991;679-686
    • (1991) J. Mol. Biol. , vol.222 , pp. 679-686
    • Goto, Y.1    Nishikiori, S.2
  • 15
    • 0028174361 scopus 로고
    • Energetics of the alpha-lactalbumin states. a calorimetric and statistical thermodynamic study
    • Griko Y., Freire E., Privalov P.L. Energetics of the alpha-lactalbumin states. A calorimetric and statistical thermodynamic study. Biochemistry. 33:1994;1889-1899
    • (1994) Biochemistry , vol.33 , pp. 1889-1899
    • Griko, Y.1    Freire, E.2    Privalov, P.L.3
  • 16
  • 17
    • 0030580089 scopus 로고    scopus 로고
    • Structure based calculation of the equilibrium folding pathway of proteins. Correlation with hydrogen exchange protection factors
    • Hilser V.J., Freire E. Structure based calculation of the equilibrium folding pathway of proteins. Correlation with hydrogen exchange protection factors. J. Mol. Biol. 262:1996;756-772
    • (1996) J. Mol. Biol , vol.262 , pp. 756-772
    • Hilser, V.J.1    Freire, E.2
  • 18
    • 0031042186 scopus 로고    scopus 로고
    • Predicting the equilibrium protein folding pathway: Structure-based analysis of staphylococcal nuclease
    • Hilser V.J., Freire E. Predicting the equilibrium protein folding pathway structure-based analysis of staphylococcal nuclease. Proteins: Struct. Funct. Genet. 27:1997;171-183
    • (1997) Proteins: Struct. Funct. Genet. , vol.27 , pp. 171-183
    • Hilser, V.J.1    Freire, E.2
  • 19
    • 0024338305 scopus 로고
    • Use of site-directed mutagenesis to destabilize native apomyoglobin relative to folding intermediates
    • Hughson F.M., Baldwin R.L. Use of site-directed mutagenesis to destabilize native apomyoglobin relative to folding intermediates. Biochemistry. 28:1989;4415-4422
    • (1989) Biochemistry , vol.28 , pp. 4415-4422
    • Hughson, F.M.1    Baldwin, R.L.2
  • 20
    • 0025186451 scopus 로고
    • Structural characterization of a partly folded apomyoglobin intermediate
    • Hughson F.M., Wright P.E., Baldwin R.L. Structural characterization of a partly folded apomyoglobin intermediate. Science. 249:1990;1544-1548
    • (1990) Science , vol.249 , pp. 1544-1548
    • Hughson, F.M.1    Wright, P.E.2    Baldwin, R.L.3
  • 21
    • 0024417964 scopus 로고
    • The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure
    • Kuwajima K. The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins: Struct. Funct. Genet. 6:1989;87-103
    • (1989) Proteins: Struct. Funct. Genet. , vol.6 , pp. 87-103
    • Kuwajima, K.1
  • 22
    • 0017178548 scopus 로고
    • Three-state denaturation of α-lactalbumin by guanidine hydrochloride
    • Kuwajima K., Nitta K., Yoneyama M., Sugai S. Three-state denaturation of α-lactalbumin by guanidine hydrochloride. J. Mol. Biol. 106:1976;359-373
    • (1976) J. Mol. Biol. , vol.106 , pp. 359-373
    • Kuwajima, K.1    Nitta, K.2    Yoneyama, M.3    Sugai, S.4
  • 23
    • 85030339093 scopus 로고    scopus 로고
    • A system for the structure-based prediction of binding affinities and molecular design of peptide ligands
    • In the press
    • Luque I., Freire E. A system for the structure-based prediction of binding affinities and molecular design of peptide ligands. Methods. Enzymol. 1997;. In the press
    • (1997) Methods. Enzymol
    • Luque, I.1    Freire, E.2
  • 24
    • 0000732609 scopus 로고
    • GRASP: Graphical representation and analysis of surface properties
    • Nicholls A., Bharadwaj R., Honig B. GRASP graphical representation and analysis of surface properties. Biophys. J. 64:1993;166-170
    • (1993) Biophys. J. , vol.64 , pp. 166-170
    • Nicholls, A.1    Bharadwaj, R.2    Honig, B.3
  • 25
    • 0028334906 scopus 로고
    • A protein dissection study of a molten globule
    • Peng Z.-y., Kim P.S. A protein dissection study of a molten globule. Biochemistry. 33:1994;2136-2141
    • (1994) Biochemistry , vol.33 , pp. 2136-2141
    • Peng, Z.-Y.1    Kim, P.S.2
  • 26
    • 0018588511 scopus 로고
    • Stability of proteins: Small globular proteins
    • Privalov P.L. Stability of proteins small globular proteins. Advan. Protein Chem. 33:1979;167-239
    • (1979) Advan. Protein Chem. , vol.33 , pp. 167-239
    • Privalov, P.L.1
  • 27
    • 0028845120 scopus 로고
    • Precise scanning calorimeter for studying thermal properties of biological macromolecules in dilute solution
    • Privalov G., Kavina V., Freire E., Privalov P.L. Precise scanning calorimeter for studying thermal properties of biological macromolecules in dilute solution. Anal. Biochem. 232:1995;79-85
    • (1995) Anal. Biochem. , vol.232 , pp. 79-85
    • Privalov, G.1    Kavina, V.2    Freire, E.3    Privalov, P.L.4
  • 28
    • 0002940127 scopus 로고
    • The molten globule state
    • T.E. Creighton. New York: Freeman
    • Ptitsyn O. The molten globule state. Creighton T.E. Protein Folding. 1992;243-300 Freeman, New York
    • (1992) Protein Folding , pp. 243-300
    • Ptitsyn, O.1
  • 29
    • 0024504662 scopus 로고
    • Solution conformation of a synthetic fragment of human pituitary growth hormone. Two-dimensional NMR of an α-helical dimer
    • Roongta V., Powers R., Jones C., Beakage M.J., Shields J.E., Gorenstein D.G. Solution conformation of a synthetic fragment of human pituitary growth hormone. Two-dimensional NMR of an α-helical dimer. Biochemistry. 28:1989;1048-1054
    • (1989) Biochemistry , vol.28 , pp. 1048-1054
    • Roongta, V.1    Powers, R.2    Jones, C.3    Beakage, M.J.4    Shields, J.E.5    Gorenstein, D.G.6
  • 30
    • 0024963569 scopus 로고
    • Residual structure in large fragments of staphylococcal nuclease: Effects of amino acid substitutions
    • Shortle D., Meeker A.K. Residual structure in large fragments of staphylococcal nuclease effects of amino acid substitutions. Biochemistry. 28:1989;936-944
    • (1989) Biochemistry , vol.28 , pp. 936-944
    • Shortle, D.1    Meeker, A.K.2
  • 31
    • 0028176911 scopus 로고
    • "partly folded" state, a new equilibrium state of protein molecules: Four state guanidinium chloride-induced unfolding of β-lactamase at low temperature
    • Uversky V.N., Ptitsyn O.B. "Partly folded" state, a new equilibrium state of protein molecules four state guanidinium chloride-induced unfolding of β-lactamase at low temperature. Biochemistry. 33:1994;2782-2791
    • (1994) Biochemistry , vol.33 , pp. 2782-2791
    • Uversky, V.N.1    Ptitsyn, O.B.2
  • 32
    • 0028856228 scopus 로고
    • The equilibrium folding pathway of staphylococcal nuclease: Identification of the most stable chain-chain interactions by NMR and CD spectroscopy
    • Wang Y., Shortle D. The equilibrium folding pathway of staphylococcal nuclease identification of the most stable chain-chain interactions by NMR and CD spectroscopy. Biochemistry. 34:1995;15895-15905
    • (1995) Biochemistry , vol.34 , pp. 15895-15905
    • Wang, Y.1    Shortle, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.