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Volumn 244, Issue 2, 1997, Pages 343-351

Conformational changes of arginine kinase induced by photochemical release of nucleotides from caged nucleotides. An infrared difference-spectroscopy investigation

Author keywords

Arginine kinase; Caged nucleotide; Conformational change; Fourier transform infrared spectroscopy; Secondary structure

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE MAGNESIUM; ARGININE; ARGININE KINASE; NITRATE;

EID: 0031045929     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.00343.x     Document Type: Article
Times cited : (19)

References (65)
  • 1
    • 0026507761 scopus 로고
    • Amide modes and protein conformation
    • Bandekar, J. (1992) Amide modes and protein conformation, Biochim. Biophys. Acta 1120, 123-143.
    • (1992) Biochim. Biophys. Acta , vol.1120 , pp. 123-143
    • Bandekar, J.1
  • 2
    • 0026030935 scopus 로고
    • Infrared spectroscopic signals arising from ligand binding and conformational changes in the catalytic cycle of sarcoplasmic reticulum calcium ATPase
    • Barth, A., Mäntele, W. & Kreutz, W. (1991) Infrared spectroscopic signals arising from ligand binding and conformational changes in the catalytic cycle of sarcoplasmic reticulum calcium ATPase, Biochim. Biophys. Acta 1057, 115-123.
    • (1991) Biochim. Biophys. Acta , vol.1057 , pp. 115-123
    • Barth, A.1    Mäntele, W.2    Kreutz, W.3
  • 3
    • 0027940230 scopus 로고
    • 2+-ATPase: Investigation of nucleotide-binding, phosphorylation and phosphoenzyme conversion by FTIR difference spectroscopy
    • 2+-ATPase: investigation of nucleotide-binding, phosphorylation and phosphoenzyme conversion by FTIR difference spectroscopy, Biochim. Biophys. Acta 1194, 75-91.
    • (1994) Biochim. Biophys. Acta , vol.1194 , pp. 75-91
    • Barth, A.1    Kreutz, W.2    Mäntele, W.3
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of proteins utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of proteins utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-251.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-251
    • Bradford, M.M.1
  • 6
    • 0016246761 scopus 로고
    • Interaction of manganous ion substrates and anions with arginine kinase
    • Buttlaire, D. H. & Cohn, M. (1974a) Interaction of manganous ion substrates and anions with arginine kinase, J. Biol. Chem. 249, 5733-5740.
    • (1974) J. Biol. Chem. , vol.249 , pp. 5733-5740
    • Buttlaire, D.H.1    Cohn, M.2
  • 7
    • 0016246760 scopus 로고
    • Characterization of the active-site structures of arginine kinase-substrate complexes
    • Buttlaire, D. H. & Cohn, M. (1974b) Characterization of the active-site structures of arginine kinase-substrate complexes, J. Biol. Chem. 249, 5741-5748.
    • (1974) J. Biol. Chem. , vol.249 , pp. 5741-5748
    • Buttlaire, D.H.1    Cohn, M.2
  • 8
    • 0022691315 scopus 로고
    • Examination of the secondary-structure of proteins by deconvolved FTIR spectra
    • Byler, M. D. & Susi, H. (1986) Examination of the secondary-structure of proteins by deconvolved FTIR spectra, Biopolymers 25, 469-487.
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, M.D.1    Susi, H.2
  • 9
    • 0016797947 scopus 로고
    • Estimation of amino acid residue side-chain absorption in the infrared spectra of protein solutions in heavy water
    • Chirgadze, Y. N., Fedorov, O. V. & Trushina, N. P. (1975) Estimation of amino acid residue side-chain absorption in the infrared spectra of protein solutions in heavy water, Biopolymers 14, 679-694.
    • (1975) Biopolymers , vol.14 , pp. 679-694
    • Chirgadze, Y.N.1    Fedorov, O.V.2    Trushina, N.P.3
  • 10
    • 0020479293 scopus 로고
    • Reactivity and metal-dependent stereospecificity of the phosphorothioate analogs of ATP in the arginine kinase reaction. Structure of the metal-nucleoside triphosphate substrate
    • Cohn, M., Shih, N. & Nick, J. (1982) Reactivity and metal-dependent stereospecificity of the phosphorothioate analogs of ATP in the arginine kinase reaction. Structure of the metal-nucleoside triphosphate substrate, J. Biol. Chem. 257, 7646-7649.
    • (1982) J. Biol. Chem. , vol.257 , pp. 7646-7649
    • Cohn, M.1    Shih, N.2    Nick, J.3
  • 11
    • 0017378118 scopus 로고
    • 2+-ATPase by a nonionic detergent
    • 2+-ATPase by a nonionic detergent, J. Biol. Chem. 252, 3551-3553.
    • (1977) J. Biol. Chem. , vol.252 , pp. 3551-3553
    • Dean, W.L.1    Tanford, C.2
  • 12
    • 0027486802 scopus 로고
    • Cloning and sequence analysis of the cDNA for arginine kinase of lobster muscle
    • Dumas, C. & Camonis, J. (1993) Cloning and sequence analysis of the cDNA for arginine kinase of lobster muscle, J. Biol. Chem. 268, 21599-21605.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21599-21605
    • Dumas, C.1    Camonis, J.2
  • 13
    • 0000219480 scopus 로고
    • Conformational changes in arginine kinase upon ligand binding seen by small-angle X-ray scattering
    • Dumas, C. & Janin, J. (1983) Conformational changes in arginine kinase upon ligand binding seen by small-angle X-ray scattering, FEBS Lett. 153, 128-130.
    • (1983) FEBS Lett. , vol.153 , pp. 128-130
    • Dumas, C.1    Janin, J.2
  • 14
    • 0015223412 scopus 로고
    • Effects of iodination and acetylation of tyrosyl residues on the activity and structure of arginine kinase from lobster muscle
    • Fattoum, A., Kassab, R. & Pradel, L.-A. (1971) Effects of iodination and acetylation of tyrosyl residues on the activity and structure of arginine kinase from lobster muscle, Eur. J. Biochem. 22, 445-456.
    • (1971) Eur. J. Biochem. , vol.22 , pp. 445-456
    • Fattoum, A.1    Kassab, R.2    Pradel, L.-A.3
  • 15
    • 21144459189 scopus 로고
    • In situ infrared attenuated total reflection (IR ATR) spectroscopy: A complementary analytical tool for drug design and drug delivery
    • Fringeli, U. P. (1992) In situ infrared attenuated total reflection (IR ATR) spectroscopy: A complementary analytical tool for drug design and drug delivery, Chimia 46, 200-214.
    • (1992) Chimia , vol.46 , pp. 200-214
    • Fringeli, U.P.1
  • 17
    • 6444222991 scopus 로고
    • Use of glass electrodes to measure acidities in deuterium oxide
    • Glasoe, P. K. & Long, F. A. (1960) Use of glass electrodes to measure acidities in deuterium oxide, J. Phys. Chem. 64, 188-190.
    • (1960) J. Phys. Chem. , vol.64 , pp. 188-190
    • Glasoe, P.K.1    Long, F.A.2
  • 18
    • 0028709095 scopus 로고
    • Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy I. Assignments and model compounds in subcellular biochemistry
    • Hilderson, H. J. & Ralston, G. B., eds Plenum Press, New York
    • Goormaghtigh, E., Cabiaux, V. & Ruysschaert, J. M. (1994) Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy I. Assignments and model compounds in subcellular biochemistry, in Physical methods in the study of biomembranes (Hilderson, H. J. & Ralston, G. B., eds) vol. 23, pp. 329-362, Plenum Press, New York.
    • (1994) Physical Methods in the Study of Biomembranes , vol.23 , pp. 329-362
    • Goormaghtigh, E.1    Cabiaux, V.2    Ruysschaert, J.M.3
  • 19
    • 0026785833 scopus 로고
    • Fourier transform infrared (FTIR) spectroscopic investigation of the nicotinic acetylcholine receptor (nAChR)
    • Görne-Tschelnokow, U., Hucho, F., Naumann, D., Barth, A. & Mäntele, W. (1992) Fourier transform infrared (FTIR) spectroscopic investigation of the nicotinic acetylcholine receptor (nAChR), FEBS Lett. 309, 213-217.
    • (1992) FEBS Lett. , vol.309 , pp. 213-217
    • Görne-Tschelnokow, U.1    Hucho, F.2    Naumann, D.3    Barth, A.4    Mäntele, W.5
  • 20
    • 0029143228 scopus 로고
    • Multi-state equilibrium unfolding of guanidino kinases
    • Gross, M., Lustig, A., Wallimann, T. & Furter, R. (1995) Multi-state equilibrium unfolding of guanidino kinases, Biochemistry 34, 10350-10357.
    • (1995) Biochemistry , vol.34 , pp. 10350-10357
    • Gross, M.1    Lustig, A.2    Wallimann, T.3    Furter, R.4
  • 21
    • 0028964333 scopus 로고
    • Protein folding intermediates with rapidely exchangeable amide protons contain authentic hydrogen-bonded secondary-structure
    • Guijarro, J. I., Jackson, M., Chaffotte, A. F., Delepierre, M., Mantsch, H. H. & Goldberg, M. E. (1995) Protein folding intermediates with rapidely exchangeable amide protons contain authentic hydrogen-bonded secondary-structure, Biochemistry 34, 2998-3008.
    • (1995) Biochemistry , vol.34 , pp. 2998-3008
    • Guijarro, J.I.1    Jackson, M.2    Chaffotte, A.F.3    Delepierre, M.4    Mantsch, H.H.5    Goldberg, M.E.6
  • 22
    • 0029002812 scopus 로고
    • The conformational analysis of peptides using Fourier transform IR spectroscopy
    • Haris, P. I. & Chapman, D. (1995) The conformational analysis of peptides using Fourier transform IR spectroscopy, Biopolymers 37, 251-263.
    • (1995) Biopolymers , vol.37 , pp. 251-263
    • Haris, P.I.1    Chapman, D.2
  • 23
    • 0028967120 scopus 로고
    • Protonation of Glu L212 following QB formation in the photosynthetic reaction center of Rhodobacter sphaeroides: Evidence from time-resolved infrared spectroscopy
    • Hienerwadel, R., Grzybeck, S., Fogel, C., Kreutz, W., Okamura, M. Y., Paddock, M. L., Breton, J., Nabedryk, E. & Mäntele, W. (1995) Protonation of Glu L212 following QB formation in the photosynthetic reaction center of Rhodobacter sphaeroides: evidence from time-resolved infrared spectroscopy, Biochemistry 34, 2832-2843.
    • (1995) Biochemistry , vol.34 , pp. 2832-2843
    • Hienerwadel, R.1    Grzybeck, S.2    Fogel, C.3    Kreutz, W.4    Okamura, M.Y.5    Paddock, M.L.6    Breton, J.7    Nabedryk, E.8    Mäntele, W.9
  • 24
    • 0029018548 scopus 로고
    • The use and misuse of FTIR spectroscopy in the determination of protein structure
    • Jackson, M. & Mantsch, H. H. (1995) The use and misuse of FTIR spectroscopy in the determination of protein structure, Crit. Rev. Biochem. Mol. Biol. 30, 95-120.
    • (1995) Crit. Rev. Biochem. Mol. Biol. , vol.30 , pp. 95-120
    • Jackson, M.1    Mantsch, H.H.2
  • 25
    • 0024471659 scopus 로고
    • 1H NMR studies of the structure of enzyme-bound substrate complexes of lobster muscle arginine kinase: Relaxation measurements with Mn(II) and Co(II)
    • 1H NMR studies of the structure of enzyme-bound substrate complexes of lobster muscle arginine kinase: relaxation measurements with Mn(II) and Co(II), Biochemistry 28, 9343-9350.
    • (1989) Biochemistry , vol.28 , pp. 9343-9350
    • Jarori, G.K.1    Ray, B.D.2    Nageswara Rao, B.D.3
  • 26
    • 0017867017 scopus 로고
    • Rapid photolytic release of adenosine 5′-triphosphate from a protected analogue: Utilization by the Na:K pump of human red blood cell ghosts
    • Kaplan, J. H., Forbush, B. III & Hoffman, J. F. (1978) Rapid photolytic release of adenosine 5′-triphosphate from a protected analogue: utilization by the Na:K pump of human red blood cell ghosts, Biochemistry 17, 1929-1935.
    • (1978) Biochemistry , vol.17 , pp. 1929-1935
    • Kaplan, J.H.1    Forbush III, B.2    Hoffman, J.F.3
  • 27
    • 0014203685 scopus 로고
    • Comparison des groupes SH réactifs des ATP : Guanidine phosphotransferases
    • Kassab, R., Pradel, A., Der Terrosian, E. & Thoai, N. V. (1967) Comparison des groupes SH réactifs des ATP : guanidine phosphotransferases, Biochim. Biophys. Acta 132, 347-360.
    • (1967) Biochim. Biophys. Acta , vol.132 , pp. 347-360
    • Kassab, R.1    Pradel, A.2    Der Terrosian, E.3    Thoai, N.V.4
  • 28
    • 17544398876 scopus 로고
    • 2 lysine essentiels avec le l-diméthylaminonaphtalène-5-sulfochlorure
    • 2 lysine essentiels avec le l-diméthylaminonaphtalène-5-sulfochlorure, Biochim. Biophys. Acta 167, 308-316.
    • (1968) Biochim. Biophys. Acta , vol.167 , pp. 308-316
    • Kassab, R.1    Roustan, C.2    Pradel, L.A.3
  • 29
    • 0023008334 scopus 로고
    • Vibrational spectroscopy and conformation of peptides, polypeptides and proteins
    • Krimm, S. & Bandekar, J. (1986) Vibrational spectroscopy and conformation of peptides, polypeptides and proteins, Adv. Protein Chem. 38, 181-386.
    • (1986) Adv. Protein Chem. , vol.38 , pp. 181-386
    • Krimm, S.1    Bandekar, J.2
  • 30
    • 0027433507 scopus 로고
    • Fourier transform infrared spectroscopic studies of the secondary-structure of spectrin under different ionic strengths
    • LaBrake, C. C., Wang, L., Keiderling, T. A. & Fung, W. N. (1993) Fourier transform infrared spectroscopic studies of the secondary-structure of spectrin under different ionic strengths, Biochemistry 32, 10296-10302.
    • (1993) Biochemistry , vol.32 , pp. 10296-10302
    • LaBrake, C.C.1    Wang, L.2    Keiderling, T.A.3    Fung, W.N.4
  • 31
    • 0015921163 scopus 로고
    • Multiple effects of ions on ATP:arginine and ATP:creatine phosphotransferases
    • Lacombe, G., Thiem, N. V. & Thoai, N. V. (1973) Multiple effects of ions on ATP:arginine and ATP:creatine phosphotransferases, Biochim. Biophys. Acta 293, 150-153.
    • (1973) Biochim. Biophys. Acta , vol.293 , pp. 150-153
    • Lacombe, G.1    Thiem, N.V.2    Thoai, N.V.3
  • 33
    • 0027316209 scopus 로고
    • Reaction-induced infrared difference spectroscopy for the study of protein function and reaction mechanisms
    • Mäntele, W. (1993) Reaction-induced infrared difference spectroscopy for the study of protein function and reaction mechanisms. Trends Biochem. Sci. 18, 197-202.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 197-202
    • Mäntele, W.1
  • 34
    • 0015052797 scopus 로고
    • Inhibition of adenosine 5′-triphosphate-creatine phosphotransferase by substrate-anion complexes
    • Milner-White, E. J. & Watts, D. C. (1971) Inhibition of adenosine 5′-triphosphate-creatine phosphotransferase by substrate-anion complexes, Biochem. J. 122, 727-740.
    • (1971) Biochem. J. , vol.122 , pp. 727-740
    • Milner-White, E.J.1    Watts, D.C.2
  • 35
    • 77956932220 scopus 로고
    • Arginine kinase and other invertebrate guanidino kinases
    • Morrison, J. F. (1973) Arginine kinase and other invertebrate guanidino kinases, Enzymes 3, 457-486.
    • (1973) Enzymes , vol.3 , pp. 457-486
    • Morrison, J.F.1
  • 37
    • 0027145125 scopus 로고
    • Two-dimensional transferred nuclear overhauser effect spectroscopy (TRNOESY) studies of nucleotide conformations in creatine kinase complexes: Effects due to weak non-specific binding
    • Murali, N., Jarori, G. K., Landy, S. B. & Nageswara Rao, B. D. (1993) Two-dimensional transferred nuclear overhauser effect spectroscopy (TRNOESY) studies of nucleotide conformations in creatine kinase complexes: effects due to weak non-specific binding, Biochemistry 32, 12941-12948.
    • (1993) Biochemistry , vol.32 , pp. 12941-12948
    • Murali, N.1    Jarori, G.K.2    Landy, S.B.3    Nageswara Rao, B.D.4
  • 38
    • 0027971493 scopus 로고
    • Two-dimensional transferred nuclear Overhauser effect spectroscopy (TRNOESY) studies of nucleotide conformations in arginine kinase complexes
    • Murali, N., Jarori, G. K. & Nageswara Rao, B. D. (1994) Two-dimensional transferred nuclear Overhauser effect spectroscopy (TRNOESY) studies of nucleotide conformations in arginine kinase complexes, Biochemistry 33, 14227-14236.
    • (1994) Biochemistry , vol.33 , pp. 14227-14236
    • Murali, N.1    Jarori, G.K.2    Nageswara Rao, B.D.3
  • 39
    • 0017368578 scopus 로고
    • 31P-NMR of bound substrates of arginine kinase reaction, chemical shifts in binary, ternary, quaternary and transition-state-analog complexes
    • 31P-NMR of bound substrates of arginine kinase reaction, chemical shifts in binary, ternary, quaternary and transition-state-analog complexes, J. Biol. Chem. 252, 3344-3350.
    • (1977) J. Biol. Chem. , vol.252 , pp. 3344-3350
    • Nageswara Rao, B.D.1    Cohn, M.2
  • 40
    • 0019394535 scopus 로고
    • 31P-NMR of enzyme-bound substrates of rabbit muscle creatine kinase equilibrium constants, interconversion rates and NMR parameters of enzyme-bound complexes
    • 31P-NMR of enzyme-bound substrates of rabbit muscle creatine kinase equilibrium constants, interconversion rates and NMR parameters of enzyme-bound complexes, J. Biol. Chem. 256, 1716-1721.
    • (1981) J. Biol. Chem. , vol.256 , pp. 1716-1721
    • Nageswara Rao, B.D.1    Cohn, M.2
  • 41
    • 0014406934 scopus 로고
    • Site actif des ATP:guanidine phosphotransférases. II. Mise en évidence de résidus histidine essentiels au moyen du pyrocarbonate d'éthyle
    • Pradel, L. A. & Kassab, R. (1968) Site actif des ATP:guanidine phosphotransférases. II. Mise en évidence de résidus histidine essentiels au moyen du pyrocarbonate d'éthyle, Biophys. Biochim. Acta 167, 317-325.
    • (1968) Biophys. Biochim. Acta , vol.167 , pp. 317-325
    • Pradel, L.A.1    Kassab, R.2
  • 42
    • 0028847259 scopus 로고
    • Effects of pH and KCl on the conformations of creatine kinase from rabbit muscle. Infrared, circular dichroic and fluorescence studies
    • Raimbault, C., Couthon, F., Vial, C. & Buchet, R. (1995) Effects of pH and KCl on the conformations of creatine kinase from rabbit muscle. Infrared, circular dichroic and fluorescence studies, Eur. J. Biochem. 234, 570-578.
    • (1995) Eur. J. Biochem. , vol.234 , pp. 570-578
    • Raimbault, C.1    Couthon, F.2    Vial, C.3    Buchet, R.4
  • 43
    • 0029820647 scopus 로고    scopus 로고
    • Changes of creatine kinase secondary-structure induced by the release of nucleotides from caged compounds. An infrared difference-spectroscopy study
    • Raimbault, C., Buchet, R. & Vial, C. (1996) Changes of creatine kinase secondary-structure induced by the release of nucleotides from caged compounds. An infrared difference-spectroscopy study, Eur. J. Biochem. 240, 134-142.
    • (1996) Eur. J. Biochem. , vol.240 , pp. 134-142
    • Raimbault, C.1    Buchet, R.2    Vial, C.3
  • 44
    • 0015523053 scopus 로고
    • Structural changes induced by substrates and anions at the active-site of creatine kinase
    • Reed, G. H. & Cohn, M. (1972) Structural changes induced by substrates and anions at the active-site of creatine kinase, J. Biol. Chem. 247, 3073-3081.
    • (1972) J. Biol. Chem. , vol.247 , pp. 3073-3081
    • Reed, G.H.1    Cohn, M.2
  • 45
    • 0026643216 scopus 로고
    • FTIR difference spectroscopy of bacteriorhodopsin: Toward a molecular model
    • Rotschild, K. J. (1992) FTIR difference spectroscopy of bacteriorhodopsin: toward a molecular model, J. Bioenerg. Biomembr. 24, 147-167.
    • (1992) J. Bioenerg. Biomembr. , vol.24 , pp. 147-167
    • Rotschild, K.J.1
  • 46
    • 0014406874 scopus 로고
    • Interactions des ATP:guanidine phosphotransférases avec leurs substrats, étudiée par spectrométrie différentielle
    • Roustan, C., Kassab, R., Pradel, L. A. & Van Thoai, N. (1968) Interactions des ATP:guanidine phosphotransférases avec leurs substrats, étudiée par spectrométrie différentielle, Biochim. Biophys. Acta 167, 326-338.
    • (1968) Biochim. Biophys. Acta , vol.167 , pp. 326-338
    • Roustan, C.1    Kassab, R.2    Pradel, L.A.3    Van Thoai, N.4
  • 47
    • 0015138957 scopus 로고
    • Studies on the partial exchange and overall reactions catalyzed by native and modified arginine kinase from Homarus vulgaris muscle
    • Roustan, C., Pradel, L. A., Kassab, R. & Thoai, N. V. (1971) Studies on the partial exchange and overall reactions catalyzed by native and modified arginine kinase from Homarus vulgaris muscle, Biochim. Biophys. Acta 250, 103-116.
    • (1971) Biochim. Biophys. Acta , vol.250 , pp. 103-116
    • Roustan, C.1    Pradel, L.A.2    Kassab, R.3    Thoai, N.V.4
  • 49
    • 0025906210 scopus 로고
    • Protein structure from Fourier transform infrared spectroscopy: A data base analysis
    • Sarver, R. W. & Krueger, W. C. (1991) Protein structure from Fourier transform infrared spectroscopy: a data base analysis, Anal. Biochem. 194, 89-100.
    • (1991) Anal. Biochem. , vol.194 , pp. 89-100
    • Sarver, R.W.1    Krueger, W.C.2
  • 50
    • 0028944068 scopus 로고
    • Nanosecond time-resolved infrared spectroscopy distinguishes two K species in the bacteriorhodopsin photocycle
    • Sasaki, J., Yuzawa, T., Kandori, H., Maeda, A. & Hamaguchi, H. (1995) Nanosecond time-resolved infrared spectroscopy distinguishes two K species in the bacteriorhodopsin photocycle, Biophys. J. 68, 2073-2080.
    • (1995) Biophys. J. , vol.68 , pp. 2073-2080
    • Sasaki, J.1    Yuzawa, T.2    Kandori, H.3    Maeda, A.4    Hamaguchi, H.5
  • 51
    • 0000404051 scopus 로고
    • Conformations and orientations of amphilic peptides induced by artificial lipid membranes: Correlation with biological activity
    • Schwyzer, R. (1992) Conformations and orientations of amphilic peptides induced by artificial lipid membranes: correlation with biological activity, Chemtracts Biochem. Mol. Biol. 3, 347-379.
    • (1992) Chemtracts Biochem. Mol. Biol. , vol.3 , pp. 347-379
    • Schwyzer, R.1
  • 52
    • 0000876678 scopus 로고
    • Infrared spectra of nucleic acids and related compounds
    • Shimanouchi, T., Tsuboi, M. & Kyogoku, Y. (1964) Infrared spectra of nucleic acids and related compounds, Adv. Chem. Phys. 7, 435-496.
    • (1964) Adv. Chem. Phys. , vol.7 , pp. 435-496
    • Shimanouchi, T.1    Tsuboi, M.2    Kyogoku, Y.3
  • 53
    • 0028909764 scopus 로고
    • Infrared spectroscopy applied to biochemical and biological problems
    • Siebert, F. (1995) Infrared spectroscopy applied to biochemical and biological problems, Methods Enzymol. 246, 501-526.
    • (1995) Methods Enzymol. , vol.246 , pp. 501-526
    • Siebert, F.1
  • 54
    • 0015240572 scopus 로고
    • Effect of substrate analogues on the kinetics of the reaction catalyzed by adenosine triphosphate : Arginine phosphotransferase
    • Smith, E. & Morrison, J. F. (1971) Effect of substrate analogues on the kinetics of the reaction catalyzed by adenosine triphosphate : arginine phosphotransferase, J. Biol. Chem. 246, 7764-7772.
    • (1971) J. Biol. Chem. , vol.246 , pp. 7764-7772
    • Smith, E.1    Morrison, J.F.2
  • 55
    • 0028858939 scopus 로고
    • Isolation and sequence analysis of the gene for arginine kinase from the chelicerate arthropod, Limulus polyphemus: Insights into catalytically important residue
    • Strong, S. J. & Ellington, W. R. (1995) Isolation and sequence analysis of the gene for arginine kinase from the chelicerate arthropod, Limulus polyphemus: insights into catalytically important residue, Biochim. Biophys. Acta 1246, 197-200.
    • (1995) Biochim. Biophys. Acta , vol.1246 , pp. 197-200
    • Strong, S.J.1    Ellington, W.R.2
  • 56
    • 0023837785 scopus 로고
    • New insight into protein secondary-structure from resolution-enhanced infrared spectra
    • Surewicz, W. K. & Mantsch, H. H. (1988) New insight into protein secondary-structure from resolution-enhanced infrared spectra, Biochim. Biophys. Acta 952, 115-130.
    • (1988) Biochim. Biophys. Acta , vol.952 , pp. 115-130
    • Surewicz, W.K.1    Mantsch, H.H.2
  • 57
    • 0027492164 scopus 로고
    • Determination of protein secondary-structure by Fourier transform infrared spectroscopy: A critical assessment
    • Surewicz, W. K., Mantsch, H. H. & Chapman, D. (1993) Determination of protein secondary-structure by Fourier transform infrared spectroscopy: a critical assessment, Biochemistry 32, 389-394.
    • (1993) Biochemistry , vol.32 , pp. 389-394
    • Surewicz, W.K.1    Mantsch, H.H.2    Chapman, D.3
  • 58
    • 0015438002 scopus 로고
    • Infrared spectroscopy-conformations
    • Susi, H. (1972) Infrared spectroscopy-conformations, Methods Enzymol. 26, 455-472.
    • (1972) Methods Enzymol. , vol.26 , pp. 455-472
    • Susi, H.1
  • 59
    • 0028212764 scopus 로고
    • Evolution of phosphagen kinase. Primary structure of glycocyamine kinase and arginine kinase from invertebrates
    • Suzuki, T. & Furukohori, T. (1994) Evolution of phosphagen kinase. Primary structure of glycocyamine kinase and arginine kinase from invertebrates, J. Mol. Biol. 237, 353-357.
    • (1994) J. Mol. Biol. , vol.237 , pp. 353-357
    • Suzuki, T.1    Furukohori, T.2
  • 60
    • 0019060881 scopus 로고
    • Cryoenzymic studies on the transition-state analog complex creatine kinase · ADPMg · nitrate · creatine
    • Travers, F. & Barman, T. E. (1980) Cryoenzymic studies on the transition-state analog complex creatine kinase · ADPMg · nitrate · creatine, Eur. J. Biochem. 110, 405-412.
    • (1980) Eur. J. Biochem. , vol.110 , pp. 405-412
    • Travers, F.1    Barman, T.E.2
  • 61
    • 0018987703 scopus 로고
    • Photoaffinity labelling of arginine kinase and creatine kinase with a γ-P-substituted arylazido analogue of ATP
    • Vandest, P., Labbe, J.-P. & Kassab, R. (1980) Photoaffinity labelling of arginine kinase and creatine kinase with a γ-P-substituted arylazido analogue of ATP, Eur. J. Biochem. 104, 433-442.
    • (1980) Eur. J. Biochem. , vol.104 , pp. 433-442
    • Vandest, P.1    Labbe, J.-P.2    Kassab, R.3
  • 62
    • 0025613794 scopus 로고
    • 2O) solutions, I. Spectral parameters of amino acid residue absorption band
    • 2O) solutions, I. Spectral parameters of amino acid residue absorption band, Biopolymers 30, 1243-1257.
    • (1990) Biopolymers , vol.30 , pp. 1243-1257
    • Venyaminov, S.Y.1    Kalnin, N.N.2
  • 63
    • 77956904558 scopus 로고
    • Creatine kinase (adenosine 5′-triphosphate-creatine phosphotransferase)
    • Watts, D. C. (1973) Creatine kinase (adenosine 5′-triphosphate-creatine phosphotransferase), Enzymes 8, 383-455.
    • (1973) Enzymes , vol.8 , pp. 383-455
    • Watts, D.C.1
  • 64
    • 0028783570 scopus 로고
    • Influence of the 9-methyl group of retinal on the photocycle of bacteriorhodopsin studied by lime-resolved rapid scan and static low-temperature Fourier transform infrared difference spectroscopy
    • Weidlich, O., Friedman, N., Sheves, M. & Siebert, F. (1995) Influence of the 9-methyl group of retinal on the photocycle of bacteriorhodopsin studied by lime-resolved rapid scan and static low-temperature Fourier transform infrared difference spectroscopy, Biochemistry 34, 13502-13510.
    • (1995) Biochemistry , vol.34 , pp. 13502-13510
    • Weidlich, O.1    Friedman, N.2    Sheves, M.3    Siebert, F.4
  • 65
    • 0029075013 scopus 로고
    • Re-evaluation of the structure and physiological function of guanidino kinases in fruitfly (Drosophila), sea urchin (Psammechinus miliaris) and man
    • Wyss, M., Maughan, D. & Wallimann, T. (1995) Re-evaluation of the structure and physiological function of guanidino kinases in fruitfly (Drosophila), sea urchin (Psammechinus miliaris) and man, Biochem. J. 309, 255-261.
    • (1995) Biochem. J. , vol.309 , pp. 255-261
    • Wyss, M.1    Maughan, D.2    Wallimann, T.3


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