메뉴 건너뛰기




Volumn 38, Issue 30, 1999, Pages 9783-9790

Putative interhelix ion Pairs involved in the stability of myoglobin

Author keywords

[No Author keywords available]

Indexed keywords

CYANOMYOGLOBIN; MYOGLOBIN; SODIUM CHLORIDE; UNCLASSIFIED DRUG; UREA;

EID: 0033609475     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9828627     Document Type: Article
Times cited : (44)

References (39)
  • 2
    • 0032488654 scopus 로고    scopus 로고
    • Energetics of polar side-chain interactions in helical peptides: Salt effects on ions pairs and hydrogen bonds
    • Smith, J. S., and Scholtz, J. M. (1998). Energetics of polar side-chain interactions in helical peptides: salt effects on ions pairs and hydrogen bonds. Biochemistry 37, 33-40.
    • (1998) Biochemistry , vol.37 , pp. 33-40
    • Smith, J.S.1    Scholtz, J.M.2
  • 3
    • 0031042074 scopus 로고    scopus 로고
    • Ion-pair and charged hydrogen-bond interactions between histidine and aspartate in a peptide helix
    • Huyghues-Despointes, B., and Baldwin, R. L. (1997). Ion-pair and charged hydrogen-bond interactions between histidine and aspartate in a peptide helix. Biochemistry 36, 1965-1970.
    • (1997) Biochemistry , vol.36 , pp. 1965-1970
    • Huyghues-Despointes, B.1    Baldwin, R.L.2
  • 4
    • 0028361968 scopus 로고
    • Structural origins of pH and ionic strength effects on protein stability. Acid denaturation of sperm whale myoglobin
    • Yang, A.-S., and Honig, B. (1994). Structural origins of pH and ionic strength effects on protein stability. Acid denaturation of sperm whale myoglobin. J. Mol. Biol. 237, 602-614.
    • (1994) J. Mol. Biol. , vol.237 , pp. 602-614
    • Yang, A.-S.1    Honig, B.2
  • 5
    • 0029981924 scopus 로고    scopus 로고
    • Packing interactions in the apomyoglobin folding intermediate
    • Kay, M. S., and Baldwin, R. L. (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
  • 6
    • 0020474627 scopus 로고
    • Effect on protein stability of reversing the charge on amino groups
    • Hollecker, M., and Creighton, T. E. (1982). Effect on protein stability of reversing the charge on amino groups. Biochim. Biophys. Acta 701, 395-404.
    • (1982) Biochim. Biophys. Acta , vol.701 , pp. 395-404
    • Hollecker, M.1    Creighton, T.E.2
  • 7
    • 0029967068 scopus 로고    scopus 로고
    • Contributions of the ionizable amino acids to the stability of staphylococcal nuclease
    • Meeker, A. K., Garcia-Moreno, B., and Shortle, D. (1996). Contributions of the ionizable amino acids to the stability of staphylococcal nuclease. Biochemistry 35, 6443-6449.
    • (1996) Biochemistry , vol.35 , pp. 6443-6449
    • Meeker, A.K.1    Garcia-Moreno, B.2    Shortle, D.3
  • 8
    • 0023462496 scopus 로고
    • High-level expression of sperm whale myoglobin in Escherichia coli
    • Springer, B. A., and Sligar, S. G. (1987). High-level expression of sperm whale myoglobin in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 84, 8961-8965.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 8961-8965
    • Springer, B.A.1    Sligar, S.G.2
  • 9
    • 0029014386 scopus 로고
    • Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway
    • Loh, S. N., Kay, M. S., and Baldwin, R. L. (1995). Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway. Proc. Natl. Acad. Sci. U.S.A. 92, 5446-5450.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 5446-5450
    • Loh, S.N.1    Kay, M.S.2    Baldwin, R.L.3
  • 10
    • 49749194276 scopus 로고
    • Studies on the structure of hemoglobin. I. Physicochemical properties of human globin
    • Rossi-Fanelli, A., Antonini, E., and Caputo, A. (1958). Studies on the structure of hemoglobin. I. 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
  • 11
    • 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
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 277, 680-685.
    • (1970) Nature , vol.277 , pp. 680-685
    • Laemmli, U.K.1
  • 13
    • 0028235775 scopus 로고
    • Molecular mechanism of acid denaturation: The role of histidine residues in the partial unfolding of apomyoglobin
    • Barrick, D., Hughson, F. M., and Baldwin, R. L. (1994). Molecular mechanism of acid denaturation: The role of histidine residues in the partial unfolding of apomyoglobin. J. Mol. Biol. 237, 588-601.
    • (1994) J. Mol. Biol. , vol.237 , pp. 588-601
    • Barrick, D.1    Hughson, F.M.2    Baldwin, R.L.3
  • 14
    • 0032568639 scopus 로고    scopus 로고
    • Alternative models for describing the acid unfolding of the apomyoglobin folding intermediate
    • Kay, M. S., and Baldwin, R. L. (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
  • 16
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace, C. N. (1986). Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131, 266-280.
    • (1986) Methods Enzymol. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 17
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants
    • Santoro, M. M., and Bolen, D. W. (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
  • 18
    • 0029061516 scopus 로고
    • Protein stability as a function of denaturant concentration: The thermal stability of barnase in the presence of urea
    • Johnson, C. M., and Fersht, A. R. (1995). Protein stability as a function of denaturant concentration: the thermal stability of barnase in the presence of urea. Biochemistry 34, 6795-6804.
    • (1995) Biochemistry , vol.34 , pp. 6795-6804
    • Johnson, C.M.1    Fersht, A.R.2
  • 19
    • 0032549072 scopus 로고    scopus 로고
    • Two forms of the pH 4 folding intermediate of apomyoglobin
    • Jamin, M., and Baldwin, R. L. (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
  • 20
    • 0017364269 scopus 로고
    • Structure of myoglobin refined at 2.0 Å resolution I. Crystallographic refinement of metmyoglobin from sperm whale
    • Takano, T. (1977). Structure of myoglobin refined at 2.0 Å resolution I. Crystallographic refinement of metmyoglobin from sperm whale. J. Mol. Biol. 110, 537-568.
    • (1977) J. Mol. Biol. , vol.110 , pp. 537-568
    • Takano, T.1
  • 21
    • 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, B. F., and Baldwin, R. L. (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
  • 22
    • 0029737827 scopus 로고    scopus 로고
    • The stability of holomyoglobin is determined by heme affinity
    • Hargrove, M. S., and Olson, J. (1996). The stability of holomyoglobin is determined by heme affinity. Biochemistry 35, 11310-11318.
    • (1996) Biochemistry , vol.35 , pp. 11310-11318
    • Hargrove, M.S.1    Olson, J.2
  • 23
    • 0022994226 scopus 로고
    • Mutant forms of staphylococcal nuclease with altered patterns of guanidine hydrochloride and urea denaturation
    • Shortle, D., and Meeker A. K. (1986). Mutant forms of staphylococcal nuclease with altered patterns of guanidine hydrochloride and urea denaturation. Proteins 1, 81-89.
    • (1986) Proteins , vol.1 , pp. 81-89
    • Shortle, D.1    Meeker, A.K.2
  • 24
    • 0030032461 scopus 로고    scopus 로고
    • The denatured state (the other half of the folding equation) and its role in protein stability
    • Shortle, D. (1996). The denatured state (the other half of the folding equation) and its role in protein stability. FASEB J 10, 27-34.
    • (1996) FASEB J , vol.10 , pp. 27-34
    • Shortle, D.1
  • 25
    • 0030022713 scopus 로고    scopus 로고
    • Thermodynamics of denaturation of staphylococcal nuclease mutants: An intermediate state in protein folding
    • Carra, J. H., and Privalov, P. L. (1996). Thermodynamics of denaturation of staphylococcal nuclease mutants: an intermediate state in protein folding. FASEB J. 10, 67-74.
    • (1996) FASEB J. , vol.10 , pp. 67-74
    • Carra, J.H.1    Privalov, P.L.2
  • 26
    • 0031808804 scopus 로고    scopus 로고
    • Chemical denaturation: Potential impact of undetected intermediates in the free energy of unfolding and m-values obtained from a two-state assumption
    • Soulages, J. L. (1998). Chemical denaturation: potential impact of undetected intermediates in the free energy of unfolding and m-values obtained from a two-state assumption. Biophys. J. 75, 484-492.
    • (1998) Biophys. J. , vol.75 , pp. 484-492
    • Soulages, J.L.1
  • 27
    • 0032558991 scopus 로고    scopus 로고
    • Monitoring the sizes of denatured ensembles of staphylococcal nuclease proteins: Implications regarding m values, intermediates, and thermodynamics
    • Baskakov, I. V., & Bolen, D, W. (1998). Monitoring the sizes of denatured ensembles of staphylococcal nuclease proteins: implications regarding m values, intermediates, and thermodynamics. Biochemistry 37, 18010-18017.
    • (1998) Biochemistry , vol.37 , pp. 18010-18017
    • Baskakov, I.V.1    Bolen, D.2
  • 28
    • 0030694241 scopus 로고    scopus 로고
    • Cooperativity of folding of the apomyoglobin pH 4 intermediate studied by glycine and proline mutations
    • Luo, Y., Kay, M. S., and Baldwin, R. L. (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
  • 29
    • 0033514920 scopus 로고    scopus 로고
    • Specificity of nativelike interhelical hydrophobic contacts in the apomyoglobin intermediate
    • Kay, M. S., Ramos, C. H. I., and Baldwin, R. L, (1999). Specificity of nativelike interhelical hydrophobic contacts in the apomyoglobin intermediate. Proc. Natl, Acad. Sci. U.S.A. 96, 2007-2012.
    • (1999) Proc. Natl, Acad. Sci. U.S.A. , vol.96 , pp. 2007-2012
    • Kay, M.S.1    Ramos, C.H.I.2    Baldwin, R.L.3
  • 31
    • 0025234587 scopus 로고
    • pH-induced denaturation of proteins: A single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme
    • Anderson, D. E., Becktel, W. J., and Dahlquist, F. W. (1990). pH-induced denaturation of proteins: a single salt bridge contributes 3-5 kcal/mol to the free energy of folding of T4 lysozyme. Biochemistry 29, 2403-2408.
    • (1990) Biochemistry , vol.29 , pp. 2403-2408
    • Anderson, D.E.1    Becktel, W.J.2    Dahlquist, F.W.3
  • 32
    • 0030067976 scopus 로고    scopus 로고
    • Importance of two buried salt bridges in the stability and folding pathway of barnase
    • Tissot, A. C., Vuilleumier, S., and Fersht, A. R. (1996). Importance of two buried salt bridges in the stability and folding pathway of barnase. Biochemistry 35, 6786-6794.
    • (1996) Biochemistry , vol.35 , pp. 6786-6794
    • Tissot, A.C.1    Vuilleumier, S.2    Fersht, A.R.3
  • 33
    • 0029564595 scopus 로고    scopus 로고
    • Are buried salt bridges important for protein stability and conformational specificity?
    • Waldburger, C. D., Schildbach, J. F., and Sauer, R. T. (1996). Are buried salt bridges important for protein stability and conformational specificity? Nat. Struct. Biol. 2, 122-128.
    • (1996) Nat. Struct. Biol. , vol.2 , pp. 122-128
    • Waldburger, C.D.1    Schildbach, J.F.2    Sauer, R.T.3
  • 34
    • 0031764838 scopus 로고    scopus 로고
    • Surface salt bridges stabilize the GCN4 leucine zipper
    • Spek, E. J., Bui, A. H., Lu, M., and Kallenbach, N. R. (1998). Surface salt bridges stabilize the GCN4 leucine zipper. Protein Sci. 7, 2431-2437.
    • (1998) Protein Sci. , vol.7 , pp. 2431-2437
    • Spek, E.J.1    Bui, A.H.2    Lu, M.3    Kallenbach, N.R.4
  • 35
    • 0032011351 scopus 로고    scopus 로고
    • What ultrastable globular proteins teach us about protein stabilization
    • Jaenicke, R. (1998). What ultrastable globular proteins teach us about protein stabilization. Biochemistry (Moscow) 63, 312-321.
    • (1998) Biochemistry (Moscow) , vol.63 , pp. 312-321
    • Jaenicke, R.1
  • 36
    • 0025271463 scopus 로고
    • pH dependence of the urea and guanidine hydrochloride denaturation of ribonuclease A and ribonuclease T1
    • Pace, C. N., Laurents, D. V. Thomson, J. A. (1990). pH dependence of the urea and guanidine hydrochloride denaturation of ribonuclease A and ribonuclease T1. Biochemistry 29, 2564-2572.
    • (1990) Biochemistry , vol.29 , pp. 2564-2572
    • Pace, C.N.1    Laurents, D.V.2    Thomson, J.A.3
  • 37
    • 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, and Bolen, D, W. (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
  • 38
    • 0000808942 scopus 로고
    • The folding, stability and dynamics of T4 lysozyme: A perspective using nuclear magnetic resonance
    • (Clore, G. M., and Gronenborn, A. M., Eds.) CRC Press, Boca Raton, FL
    • Anderson, D. E., Lu, J., McIntosh, L., and Dahlquist, F. W. (1993). The folding, stability and dynamics of T4 lysozyme: a perspective using nuclear magnetic resonance, in NMR of proteins (Topics in molecular and structural biology) (Clore, G. M., and Gronenborn, A. M., Eds.) pp 258-304, CRC Press, Boca Raton, FL.
    • (1993) NMR of Proteins (Topics in Molecular and Structural Biology) , pp. 258-304
    • Anderson, D.E.1    Lu, J.2    McIntosh, L.3    Dahlquist, F.W.4
  • 39
    • 0033594989 scopus 로고    scopus 로고
    • Thermal versus guanidine-induced unfolding of ubiquitin. An analysis in terms of the contributions from charge-charge interactions to protein stability
    • in press
    • Ibarra-Molero, B., Loladze, V. V., Makhatzdze, G. I., and Sanchez-Ruiz, J. M. (1999), Thermal versus guanidine-induced unfolding of ubiquitin. An analysis in terms of the contributions from charge-charge interactions to protein stability. Biochemistry 38, in press.
    • (1999) Biochemistry , vol.38
    • Ibarra-Molero, B.1    Loladze, V.V.2    Makhatzdze, G.I.3    Sanchez-Ruiz, J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.