메뉴 건너뛰기




Volumn 270, Issue 23, 2003, Pages 4606-4614

Protein stabilization by compatible solutes: Effect of diglycerol phosphate on the dynamics of Desulfovibrio gigas rubredoxin studied by NMR

Author keywords

Chemical exchange; Compatible solutes; Protein dynamics; Rubredoxin; Thermostability

Indexed keywords

DIGLYCEROL PHOSPHATE; GLYCEROL DERIVATIVE; HYDROGEN; RUBREDOXIN; UNCLASSIFIED DRUG;

EID: 0344393574     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03861.x     Document Type: Article
Times cited : (44)

References (56)
  • 1
    • 0001912876 scopus 로고
    • Thermoadaptation of methanogenic bacteria by intracellular ion concentration
    • Hensel, R. & König, H. (1988) Thermoadaptation of methanogenic bacteria by intracellular ion concentration. FEMS Microbiol. Lett. 49, 75-79.
    • (1988) FEMS Microbiol. Lett. , vol.49 , pp. 75-79
    • Hensel, R.1    König, H.2
  • 2
    • 0000558667 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenases from archaea: Objects for studying protein thermoadaptation
    • Hensel, R., Fabry, S., Biro, J., Bogedain, C., Jakob, I. & Siebers, B. (1994) Glyceraldehyde-3-phosphate dehydrogenases from archaea: objects for studying protein thermoadaptation. Biocatalysis 11, 151-164.
    • (1994) Biocatalysis , vol.11 , pp. 151-164
    • Hensel, R.1    Fabry, S.2    Biro, J.3    Bogedain, C.4    Jakob, I.5    Siebers, B.6
  • 3
    • 0031613817 scopus 로고    scopus 로고
    • An overview of the role and diversity of compatible solutes in Bacteria and Archaea
    • da Costa, M.S., Santos, H. & Galinski, E.A. (1998) An overview of the role and diversity of compatible solutes in Bacteria and Archaea. Adv. Biochem. Eng. Biotechnol. 61, 117-153.
    • (1998) Adv. Biochem. Eng. Biotechnol. , vol.61 , pp. 117-153
    • Da Costa, M.S.1    Santos, H.2    Galinski, E.A.3
  • 4
    • 0034981263 scopus 로고    scopus 로고
    • Organic solutes from thermophiles and hyperthermophiles
    • Santos, H. & da Costa, M.S. (2001) Organic solutes from thermophiles and hyperthermophiles. Methods Enzymol. 334, 302-315.
    • (2001) Methods Enzymol. , vol.334 , pp. 302-315
    • Santos, H.1    Da Costa, M.S.2
  • 5
    • 0026766429 scopus 로고
    • Di-myo-inositol-1,1′-phosphate: A new inositol phosphate isolated from Pyrococcus woesei
    • Scholz, S., Sonnenbichler, J., Schäfer, W. & Hensel, R. (1992) Di-myo-inositol-1,1′-phosphate: a new inositol phosphate isolated from Pyrococcus woesei. FEBS Lett. 306, 239-242.
    • (1992) FEBS Lett. , vol.306 , pp. 239-242
    • Scholz, S.1    Sonnenbichler, J.2    Schäfer, W.3    Hensel, R.4
  • 8
    • 0036599177 scopus 로고    scopus 로고
    • Comparative study of the thermostabilizing properties of mannosylglycerate and other compatible solutes on model enzymes
    • Borges, N., Ramos, A., Raven, N.D., Sharp, R.J. & Santos, H. (2002) Comparative study of the thermostabilizing properties of mannosylglycerate and other compatible solutes on model enzymes. Extremophiles 6, 209-216.
    • (2002) Extremophiles , vol.6 , pp. 209-216
    • Borges, N.1    Ramos, A.2    Raven, N.D.3    Sharp, R.J.4    Santos, H.5
  • 9
    • 0029792830 scopus 로고    scopus 로고
    • How Hofmeister ion interactions affect protein stability?
    • Baldwin, R.L. (1996) How Hofmeister ion interactions affect protein stability? Biophys. J. 71, 2056-2063.
    • (1996) Biophys. J. , vol.71 , pp. 2056-2063
    • Baldwin, R.L.1
  • 10
    • 0032560503 scopus 로고    scopus 로고
    • In disperse solution, 'osmotic stress' is a restricted case of preferential interactions
    • Timasheff, S.N. (1998) In disperse solution, 'osmotic stress' is a restricted case of preferential interactions. Proc. Natl Acad. Sci. USA 95, 7363-7367.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 7363-7367
    • Timasheff, S.N.1
  • 12
    • 0020790862 scopus 로고
    • Preferential interactions of proteins with solvent components in aqueous amino acid solutions
    • Arakawa, T. & Timasheff, S.N. (1983) Preferential interactions of proteins with solvent components in aqueous amino acid solutions. Arch. Biochem. Biophys. 224, 169-177.
    • (1983) Arch. Biochem. Biophys. , vol.224 , pp. 169-177
    • Arakawa, T.1    Timasheff, S.N.2
  • 13
    • 0022032982 scopus 로고
    • The stabilization of proteins by osmolytes
    • Arakawa, T. & Timasheff, S.N. (1985) The stabilization of proteins by osmolytes. Biophys. J. 47, 411-414.
    • (1985) Biophys. J. , vol.47 , pp. 411-414
    • Arakawa, T.1    Timasheff, S.N.2
  • 14
    • 0020477047 scopus 로고
    • Preferential interactions of proteins with salts in concentrated solutions
    • Arakawa, T. & Timasheff, S.N. (1982) Preferential interactions of proteins with salts in concentrated solutions. Biochemistry 21, 6545-6552.
    • (1982) Biochemistry , vol.21 , pp. 6545-6552
    • Arakawa, T.1    Timasheff, S.N.2
  • 15
    • 0020477017 scopus 로고
    • Stabilization of protein structure by sugars
    • Arakawa, T. & Timasheff, S.N. (1982) Stabilization of protein structure by sugars. Biochemistry 21, 6536-6544.
    • (1982) Biochemistry , vol.21 , pp. 6536-6544
    • Arakawa, T.1    Timasheff, S.N.2
  • 16
    • 0021755248 scopus 로고
    • Mechanism of protein salting in and salting out by divalent cation salts: Balance between hydration and salt binding
    • Arakawa, T. & Timasheff, S.N. (1984) Mechanism of protein salting in and salting out by divalent cation salts: balance between hydration and salt binding. Biochemistry 23, 5912-5923.
    • (1984) Biochemistry , vol.23 , pp. 5912-5923
    • Arakawa, T.1    Timasheff, S.N.2
  • 17
    • 0025068721 scopus 로고
    • Why preferential hydration does not always stabilize the native structure of globular proteins
    • Arakawa, T., Bhat, R. & Timasheff, S.N. (1990) Why preferential hydration does not always stabilize the native structure of globular proteins. Biochemistry 29, 1924-1931.
    • (1990) Biochemistry , vol.29 , pp. 1924-1931
    • Arakawa, T.1    Bhat, R.2    Timasheff, S.N.3
  • 18
    • 0023505188 scopus 로고
    • Thermal stability of proteins in the presence of poly (ethylene glycols)
    • Lee, L.L. & Lee, J.C. (1987) Thermal stability of proteins in the presence of poly (ethylene glycols). Biochemistry 26, 7813-7819.
    • (1987) Biochemistry , vol.26 , pp. 7813-7819
    • Lee, L.L.1    Lee, J.C.2
  • 19
    • 0026598013 scopus 로고
    • Enzyme stabilization by ectoine-type compatible solutes: Protection against heating, freezing and drying
    • Lippert, K. & Galinski, E.A. (1992) Enzyme stabilization by ectoine-type compatible solutes: protection against heating, freezing and drying. Appl. Microbiol. Biotechnol. 37, 61-65.
    • (1992) Appl. Microbiol. Biotechnol. , vol.37 , pp. 61-65
    • Lippert, K.1    Galinski, E.A.2
  • 20
    • 0028862864 scopus 로고
    • The peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes
    • Liu, Y. & Bolen, D.W. (1995) The peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes. Biochemistry 34, 12884-12891.
    • (1995) Biochemistry , vol.34 , pp. 12884-12891
    • Liu, Y.1    Bolen, D.W.2
  • 21
    • 0032483027 scopus 로고    scopus 로고
    • Osmolyte-driven contraction of a random coil protein
    • Qu, Y., Bolen, C.L. & Bolen, D.W. (1998) Osmolyte-driven contraction of a random coil protein. Proc. Natl Acad. Sci. USA 95, 9268-9273.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 9268-9273
    • Qu, Y.1    Bolen, C.L.2    Bolen, D.W.3
  • 22
    • 0031967834 scopus 로고    scopus 로고
    • Trimethylamine-N-oxide counteracts urea effects on rabbit muscle lactate dehydrogenase function: A test of the counteraction hypothesis
    • Baskakov, I., Wang, A. & Bolen, D.W. (1998) Trimethylamine-N-oxide counteracts urea effects on rabbit muscle lactate dehydrogenase function: a test of the counteraction hypothesis. Biophys. J. 74, 2666-2673.
    • (1998) Biophys. J. , vol.74 , pp. 2666-2673
    • Baskakov, I.1    Wang, A.2    Bolen, D.W.3
  • 23
    • 0032438190 scopus 로고    scopus 로고
    • The stability of proteins in extreme environments
    • Jaenicke, R. & Böhm, G. (1998) The stability of proteins in extreme environments. Curr. Opin. Struct. Biol. 8, 738-748.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 738-748
    • Jaenicke, R.1    Böhm, G.2
  • 24
    • 0034724271 scopus 로고    scopus 로고
    • Do ultrastable proteins from hyperthermophiles have high or low conformational rigidity?
    • Jaenicke, R. (2000) Do ultrastable proteins from hyperthermophiles have high or low conformational rigidity? Proc. Natl Acad. Sci. USA 97, 2962-2964.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 2962-2964
    • Jaenicke, R.1
  • 26
    • 0018782123 scopus 로고
    • Correlation between the amide proton exchange rates and the denaturation temperatures in globular proteins related to the basic pancreatic trypsin inhibitor
    • Wagner, G. & Wüthrich, K. (1979) Correlation between the amide proton exchange rates and the denaturation temperatures in globular proteins related to the basic pancreatic trypsin inhibitor. J. Mol. Biol. 130, 31-37.
    • (1979) J. Mol. Biol. , vol.130 , pp. 31-37
    • Wagner, G.1    Wüthrich, K.2
  • 27
    • 0034724392 scopus 로고    scopus 로고
    • Millisecond time scale conformational flexibility in a hyperthermophile protein at ambient temperature
    • Hernandez, G., Jenney, F.E., Adams, M.W. & LeMaster, D.M. (2000) Millisecond time scale conformational flexibility in a hyperthermophile protein at ambient temperature. Proc. Natl Acad. Sci. USA 97, 3166-3170.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 3166-3170
    • Hernandez, G.1    Jenney, F.E.2    Adams, M.W.3    LeMaster, D.M.4
  • 28
    • 0035490249 scopus 로고    scopus 로고
    • NMR structure of Desulfovibrio gigas rubredoxin: A model for studying protein stabilization by compatible solutes
    • Lamosa, P., Brennan, L., Vis, H., Turner, D.L. & Santos, H. (2001) NMR structure of Desulfovibrio gigas rubredoxin: a model for studying protein stabilization by compatible solutes. Extremophiles 5, 303-311.
    • (2001) Extremophiles , vol.5 , pp. 303-311
    • Lamosa, P.1    Brennan, L.2    Vis, H.3    Turner, D.L.4    Santos, H.5
  • 31
    • 0028941877 scopus 로고
    • Backbone dynamics of Escherichia coli ribonuclease HI: Correlations with structure and function in an active enzyme
    • Mandel, A.M., Akke, M. & Palmer, 3rd. A.G. (1995) Backbone dynamics of Escherichia coli ribonuclease HI: correlations with structure and function in an active enzyme. J. Mol. Biol. 246, 144-163.
    • (1995) J. Mol. Biol. , vol.246 , pp. 144-163
    • Mandel, A.M.1    Akke, M.2    Palmer III, A.G.3
  • 32
    • 0035799320 scopus 로고    scopus 로고
    • 15N NMR relaxation studies of backbone dynamics in free and steroid-bound Delta 5-3-ketosteroid isomerase from Pseudomonas testosteroni
    • 15N NMR relaxation studies of backbone dynamics in free and steroid-bound Delta 5-3-ketosteroid isomerase from Pseudomonas testosteroni. Biochemistry 40, 3967-3973.
    • (2001) Biochemistry , vol.40 , pp. 3967-3973
    • Yun, S.1    Jang, D.S.2    Kim, D.H.3    Choi, K.Y.4    Lee, H.C.5
  • 33
    • 0020855355 scopus 로고
    • Hydrogen exchange and structural dynamics of proteins and nucleic acids
    • Englander, S.W. & Kallenbach, N.R. (1984) Hydrogen exchange and structural dynamics of proteins and nucleic acids. Q Rev. Biophys. 16, 521-655.
    • (1984) Q Rev. Biophys. , vol.16 , pp. 521-655
    • Englander, S.W.1    Kallenbach, N.R.2
  • 34
    • 0030612609 scopus 로고    scopus 로고
    • Hydrogen exchange: The modern legacy of Linderstrøm-Lang
    • Englander, S.W., Mayne, L., Bai, Y. & Sosnick, T.R. (1997) Hydrogen exchange: the modern legacy of Linderstrøm-Lang. Protein Sci. 6, 1101-1109.
    • (1997) Protein Sci. , vol.6 , pp. 1101-1109
    • Englander, S.W.1    Mayne, L.2    Bai, Y.3    Sosnick, T.R.4
  • 36
    • 0032478135 scopus 로고    scopus 로고
    • Effect of osmolytes on the exchange rates of backbone amide protons in proteins
    • Foord, R.L. & Leatherbarrow, R.J. (1998) Effect of osmolytes on the exchange rates of backbone amide protons in proteins. Biochemistry 37, 2969-2978.
    • (1998) Biochemistry , vol.37 , pp. 2969-2978
    • Foord, R.L.1    Leatherbarrow, R.J.2
  • 37
    • 0021919826 scopus 로고
    • A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes
    • Tabor, S. & Richardson, C.C. (1985) A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes. Proc. Natl Acad. Sci. USA 82, 1074-1078.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 1074-1078
    • Tabor, S.1    Richardson, C.C.2
  • 38
    • 0024449503 scopus 로고
    • 15N inverse detected heteronuclear NMR spectroscopy: Application to staphylococcal nuclease
    • 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease. Biochemistry 28, 8972-8979.
    • (1989) Biochemistry , vol.28 , pp. 8972-8979
    • Kay, L.E.1    Torchia, D.A.2    Bax, A.3
  • 39
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto, M., Saudek, V. & Sklenar, V. (1992) Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR 2, 661-665.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 40
    • 12044256620 scopus 로고
    • Intramolecular motions of a zinc finger DNA-binding domain from Xfin characterized by proton-detected natural abundance carbon-13 heteronuclear NMR spectroscopy
    • Palmer, 3rd, A.G., Rance, M. & Wright, P.E. (1991) Intramolecular motions of a zinc finger DNA-binding domain from Xfin characterized by proton-detected natural abundance carbon-13 heteronuclear NMR spectroscopy. J. Am. Chem. Soc. 113, 4371-4380.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 4371-4380
    • Palmer III, A.G.1    Rance, M.2    Wright, P.E.3
  • 42
    • 0035807865 scopus 로고    scopus 로고
    • Reduced temperature dependence of collective conformational opening in a hyperthermophile rubredoxin
    • Hernandez, G. & LeMaster, D.M. (2001) Reduced temperature dependence of collective conformational opening in a hyperthermophile rubredoxin. Biochemistry 40, 14384-14391.
    • (2001) Biochemistry , vol.40 , pp. 14384-14391
    • Hernandez, G.1    LeMaster, D.M.2
  • 43
    • 0026653655 scopus 로고
    • Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR
    • Englander, S.W. & Mayne, L. (1992) Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR. Annu. Rev. Biophys. Biomol. Struct. 21, 243-265.
    • (1992) Annu. Rev. Biophys. Biomol. Struct. , vol.21 , pp. 243-265
    • Englander, S.W.1    Mayne, L.2
  • 45
    • 0030822593 scopus 로고    scopus 로고
    • Stability and dynamics in a hyperthermophilic protein with melting temperature close to 200 degrees C
    • Hiller, R., Zhou, Z.H., Adams, MW. & Englander, S.W. (1997) Stability and dynamics in a hyperthermophilic protein with melting temperature close to 200 degrees C. Proc. Natl Acad. Sci. USA 94, 11329-11332.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 11329-11332
    • Hiller, R.1    Zhou, Z.H.2    Adams, M.W.3    Englander, S.W.4
  • 46
    • 0013994339 scopus 로고
    • Hydrogen exchange in proteins
    • Hvidt, A. & Nielsen, S.O. (1966) Hydrogen exchange in proteins. Adv. Protein. Chem. 21, 287-386.
    • (1966) Adv. Protein. Chem. , vol.21 , pp. 287-386
    • Hvidt, A.1    Nielsen, S.O.2
  • 47
    • 0027250665 scopus 로고
    • Primary structure effects on peptide group hydrogen exchange
    • Bai, Y., Milne, J.S., Mayne, L. & Englander, S.W. (1993) Primary structure effects on peptide group hydrogen exchange. Proteins 17. 75-86.
    • (1993) Proteins , vol.17 , pp. 75-86
    • Bai, Y.1    Milne, J.S.2    Mayne, L.3    Englander, S.W.4
  • 48
    • 0032011351 scopus 로고    scopus 로고
    • What ultrastable globular proteins teach us about protein stabilization
    • Jaenicke, R. (1997) What ultrastable globular proteins teach us about protein stabilization. Biochemystry (Moscow) 63, 312-370.
    • (1997) Biochemystry (Moscow) , vol.63 , pp. 312-370
    • Jaenicke, R.1
  • 49
    • 0038037171 scopus 로고    scopus 로고
    • Temperature dependence of anisotropic protein backbone dynamics
    • Wang, T., Cai, S. & Zuiderweg, E.R.P. (2003) Temperature dependence of anisotropic protein backbone dynamics. J. Am. Chem. Soc. 125, 8639-8643.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 8639-8643
    • Wang, T.1    Cai, S.2    Zuiderweg, E.R.P.3
  • 50
    • 0028180772 scopus 로고
    • 15N NMR relaxation studies of the FK506 binding protein: Dynamic effects of ligand binding and implications for calcineurin recognition
    • 15N NMR relaxation studies of the FK506 binding protein: dynamic effects of ligand binding and implications for calcineurin recognition. Biochemistry 33, 4093-4100.
    • (1994) Biochemistry , vol.33 , pp. 4093-4100
    • Cheng, J.W.1    Lepre, C.A.2    Moore, J.M.3
  • 52
    • 0029764317 scopus 로고    scopus 로고
    • Backbone dynamics of the C-terminal domain of Escherichia coli topoisomerase I in the absence and presence of single-stranded DNA
    • Yu, L., Zhu, C.X., Tse-Dinh, Y.C. & Fesik, S.W. (1996) Backbone dynamics of the C-terminal domain of Escherichia coli topoisomerase I in the absence and presence of single-stranded DNA. Biochemistry 35, 9661-9666.
    • (1996) Biochemistry , vol.35 , pp. 9661-9666
    • Yu, L.1    Zhu, C.X.2    Tse-Dinh, Y.C.3    Fesik, S.W.4
  • 54
    • 0030299991 scopus 로고    scopus 로고
    • 15N NMR relaxation studies of free and inhibitor-bound 4-oxalo-crotonate tautomerase: Backbone dynamics and entropy changes of an enzyme upon inhibitor binding
    • 15N NMR relaxation studies of free and inhibitor-bound 4-oxalo-crotonate tautomerase: backbone dynamics and entropy changes of an enzyme upon inhibitor binding. Biochemistry 35, 16036-16047.
    • (1996) Biochemistry , vol.35 , pp. 16036-16047
    • Stivers, J.T.1    Abeygunawardana, C.2    Mildvan, A.S.3
  • 55
    • 0034984208 scopus 로고    scopus 로고
    • NMR probes of molecular dynamics: Overview and comparison with other techniques
    • Palmer, 3rd. A.G. (2001) NMR probes of molecular dynamics: overview and comparison with other techniques. Annu. Rev. Biophys. Biomol. Struct. 30, 129-155.
    • (2001) Annu. Rev. Biophys. Biomol. Struct. , vol.30 , pp. 129-155
    • Palmer III, A.G.1
  • 56
    • 0019872622 scopus 로고
    • Mechanism of protein stabilization by glycerol: Preferential hydration in glycerol-water mixtures
    • Gekko, K. & Timasheff, S.N. (1981) Mechanism of protein stabilization by glycerol: preferential hydration in glycerol-water mixtures. Biochemistry 20, 4667-4676.
    • (1981) Biochemistry , vol.20 , pp. 4667-4676
    • Gekko, K.1    Timasheff, S.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.