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Volumn 36, Issue 49, 1997, Pages 15089-15100

Structure of the carboxy-terminal fragment of the Apo-biotin carboxyl carder subunit of Escherichia coli acetyl-CoA carboxylase

Author keywords

[No Author keywords available]

Indexed keywords

BIOTIN;

EID: 0030668421     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi971485f     Document Type: Article
Times cited : (68)

References (61)
  • 1
    • 77956910736 scopus 로고
    • Acyl-CoA Carboxylases
    • (Boyer, P. D., Ed.) Academic Press, Orlando, FL
    • Alberts, A. W., & Vagelos, P. R. (1972). Acyl-CoA Carboxylases, in The Enzymes (Boyer, P. D., Ed.) Vol. 6, pp 37-82, Academic Press, Orlando, FL.
    • (1972) The Enzymes , vol.6 , pp. 37-82
    • Alberts, A.W.1    Vagelos, P.R.2
  • 2
    • 0029646091 scopus 로고
    • Structure of the biotinyl domain of acetyl-coenzyme a carboxylase determined by MAD phasing
    • Athappilly, F. K., & Hendrickson, W. A. (1995) Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing, Structure 3, 1407-1419.
    • (1995) Structure , vol.3 , pp. 1407-1419
    • Athappilly, F.K.1    Hendrickson, W.A.2
  • 3
    • 0000913086 scopus 로고
    • A fast algorithm for rendering space-filling molecule pictures
    • Bacon, D. J., & Anderson, W. F. (1988) A fast algorithm for rendering space-filling molecule pictures, J. Mol. Graphics 6, 219-220.
    • (1988) J. Mol. Graphics , vol.6 , pp. 219-220
    • Bacon, D.J.1    Anderson, W.F.2
  • 4
    • 0000452256 scopus 로고
    • Removal of F1 baseline distortion and optimization of folding in multidimensional NMR spectra
    • Bax, A., Ikura, M., Kay, L. E., & Zhu, G. (1991) Removal of F1 baseline distortion and optimization of folding in multidimensional NMR spectra, J. Magn. Reson. 91, 174-178.
    • (1991) J. Magn. Reson. , vol.91 , pp. 174-178
    • Bax, A.1    Ikura, M.2    Kay, L.E.3    Zhu, G.4
  • 5
    • 0026748968 scopus 로고
    • 15N relaxation using inverse detected two-dimensional NMR spectroscopy: The central helix is flexible
    • 15N relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexible, Biochemistry 31, 5269-5278.
    • (1992) Biochemistry , vol.31 , pp. 5269-5278
    • Barbato, G.1    Ikura, M.2    Kay, L.E.3    Pastor, R.W.4    Bax, A.5
  • 6
    • 0027466730 scopus 로고
    • Prediction of the Three-Dimensional Structures of the Biotinylated Domain from Yeast Pyruvate Carboxylase and of the Lipoated H-protein of the Pea Leaf Glycine Cleavage System: A New Automated Method for the Prediction of Protein Tertiary Structure
    • Brocklehurst, S. M., & Perham, R. N. (1993) Prediction of the Three-Dimensional Structures of the Biotinylated Domain from Yeast Pyruvate Carboxylase and of the Lipoated H-protein of the Pea Leaf Glycine Cleavage System: A New Automated Method for the Prediction of Protein Tertiary Structure, Protein Sci. 2, 626-639.
    • (1993) Protein Sci. , vol.2 , pp. 626-639
    • Brocklehurst, S.M.1    Perham, R.N.2
  • 7
    • 0011491177 scopus 로고
    • Structure determination of a tetrasaccharide: Transient nuclear Overhauser effects in the rotating frame
    • Bothner-by, A., Stephens, R. L., Lee, J.-m., Warren, C. D., & Jeanloz, R. W. (1984) Structure determination of a tetrasaccharide: Transient nuclear Overhauser effects in the rotating frame, J. Am. Chem. Soc. 106, 811-813.
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 811-813
    • Bothner-by, A.1    Stephens, R.L.2    Lee, J.-M.3    Warren, C.D.4    Jeanloz, R.W.5
  • 8
    • 33847534249 scopus 로고
    • Effects of diffusion on free precession in nuclear magnetic resonance experiments
    • Carr, H. Y., & Purcell, E. M. (1954) Effects of diffusion on free precession in nuclear magnetic resonance experiments, Phys. Rev. 4, 630-638.
    • (1954) Phys. Rev. , vol.4 , pp. 630-638
    • Carr, H.Y.1    Purcell, E.M.2
  • 9
    • 0023475020 scopus 로고
    • Three-dimensional structure of potato carboxypeptidase inhibitor in solution. A study using nuclear magnetic resonance, distance geometry, and restrained molecular dynamics
    • Clore, G. M., Gronenborn, A. M., Nilges, M., & Ryan, C. A. (1987) Three-dimensional structure of potato carboxypeptidase inhibitor in solution. A study using nuclear magnetic resonance, distance geometry, and restrained molecular dynamics, Biochemistry 26, 8012-8023.
    • (1987) Biochemistry , vol.26 , pp. 8012-8023
    • Clore, G.M.1    Gronenborn, A.M.2    Nilges, M.3    Ryan, C.A.4
  • 10
    • 0025293361 scopus 로고
    • Biotination of Proteins in Vivo
    • Cronan, J. E., Jr., (1990) Biotination of Proteins in Vivo, J. Biol. Chem. 265, 10327-10333.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10327-10333
    • Cronan J.E., Jr.1
  • 11
    • 0025923481 scopus 로고
    • 1H-NMR Assignments and Secondary Structure of the Lipoyl Domain of the Bacillus stearothermophilus Pyruvate Dehydrogenase Multienzyme Complex
    • 1H-NMR Assignments and Secondary Structure of the Lipoyl Domain of the Bacillus stearothermophilus Pyruvate Dehydrogenase Multienzyme Complex, Eur. J. Biochem. 201, 203-209.
    • (1991) Eur. J. Biochem. , vol.201 , pp. 203-209
    • Dardel, F.1    Laue, E.D.2    Perham, R.N.3
  • 12
    • 0027340272 scopus 로고
    • Three-Dimensional Structure of the Lipoyl Domain from Bacillus stearothermophilus Pyruvate Dehydrogenase Multienzyme Complex
    • Dardel, F., Davis, A. L., Laue, E. D., & Perham, R. N. (1993) Three-Dimensional Structure of the Lipoyl Domain from Bacillus stearothermophilus Pyruvate Dehydrogenase Multienzyme Complex. J. Mol. Biol. 229, 1037-1048.
    • (1993) J. Mol. Biol. , vol.229 , pp. 1037-1048
    • Dardel, F.1    Davis, A.L.2    Laue, E.D.3    Perham, R.N.4
  • 13
    • 0014878932 scopus 로고
    • Enzymatic Carboxylation of Biotin: Molecular and Catalytic Properties of a Component Enzyme of Acetyl-Coa Carboxylase
    • Dimroth, P., Guchait, R. B., Stoll, E., & Lane, M. D. (1970) Enzymatic Carboxylation of Biotin: Molecular and Catalytic Properties of a Component Enzyme of Acetyl-CoA Carboxylase, Proc. Natl. Acad. Sci. U.S.A. 67, 1353-1360.
    • (1970) Proc. Natl. Acad. Sci. U.S.A. , vol.67 , pp. 1353-1360
    • Dimroth, P.1    Guchait, R.B.2    Stoll, E.3    Lane, M.D.4
  • 14
    • 0018369848 scopus 로고
    • Analysis of Microbial Biotin Proteins
    • Fall, R. R. (1979) Analysis of Microbial Biotin Proteins, Methods Enzymol. 62, 390-398.
    • (1979) Methods Enzymol. , vol.62 , pp. 390-398
    • Fall, R.R.1
  • 16
    • 0029071184 scopus 로고
    • Three-Dimensional Structure of a Lipoyl Domain from the Dihydrolipoyl Acetyltransferase Component of the Pyruvate Dehydrogenase Multienzyme Complex of Escherichia coli
    • Green, J. D. F., Laue, E. D., Perham, R. N., Ali, S. T., & Guest, J. R. (1995) Three-Dimensional Structure of a Lipoyl Domain from the Dihydrolipoyl Acetyltransferase Component of the Pyruvate Dehydrogenase Multienzyme Complex of Escherichia coli, J. Mol. Biol. 248, 328-343.
    • (1995) J. Mol. Biol. , vol.248 , pp. 328-343
    • Green, J.D.F.1    Laue, E.D.2    Perham, R.N.3    Ali, S.T.4    Guest, J.R.5
  • 18
    • 0027787894 scopus 로고
    • 2O in Protein NMR. Application to Sensitivity Enhancement and NOE Measurement
    • 2O in Protein NMR. Application to Sensitivity Enhancement and NOE Measurement, J. Am. Chem. Soc. 115, 12593-12593.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 12593-12593
    • Grzesiek, S.1    Bax, A.2
  • 19
    • 0016285541 scopus 로고
    • Acetyl Coenzyme a Carboxylase System of Escherichia coli: Purification and Properties of the Biotin Carboxylase, Carboxyltransferase, and Carboxyl Carrier Protein Components
    • Guchhait, R. B., Polakis, S. E., Dimroth, P., Stoll, E., Moss, J., & Lane, M. D., (1974) Acetyl Coenzyme A Carboxylase System of Escherichia coli: Purification and Properties of the Biotin Carboxylase, Carboxyltransferase, and Carboxyl Carrier Protein Components, J. Biol. Chem. 249, 6633-6645.
    • (1974) J. Biol. Chem. , vol.249 , pp. 6633-6645
    • Guchhait, R.B.1    Polakis, S.E.2    Dimroth, P.3    Stoll, E.4    Moss, J.5    Lane, M.D.6
  • 20
    • 0026259488 scopus 로고
    • Improved Efficiency of Protein Structure Calculations from NMR Data Using the Program DIANA with Redundant Dihedral Angle Constraints
    • Güntert, P., & Wüthrich, K. (1991) Improved Efficiency of Protein Structure Calculations from NMR Data Using the Program DIANA with Redundant Dihedral Angle Constraints. J. Biomol. NMR 1, 447-456.
    • (1991) J. Biomol. NMR , vol.1 , pp. 447-456
    • Güntert, P.1    Wüthrich, K.2
  • 21
    • 0026089657 scopus 로고
    • Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA
    • Güntert, P., Braun, W., & Wüthrich, K. (1991) Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA, J. Mol. Biol. 217, 517-530.
    • (1991) J. Mol. Biol. , vol.217 , pp. 517-530
    • Güntert, P.1    Braun, W.2    Wüthrich, K.3
  • 22
    • 34249765651 scopus 로고
    • NMRview: A computer program for the visualization and analysis for NMR data
    • Johnson, B. A., & Blevins, R. A. (1994) NMRview: a computer program for the visualization and analysis for NMR data, J. Biomol. NMR 4, 603-614.
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 23
    • 0003026536 scopus 로고
    • Practical aspects of 3D heteronuclear NMR of proteins
    • Kay, L. E., Marion, D., & Bax, A. (1989a) Practical aspects of 3D heteronuclear NMR of proteins, J. Magn. Reson. 84, 72-84.
    • (1989) J. Magn. Reson. , vol.84 , pp. 72-84
    • Kay, L.E.1    Marion, D.2    Bax, A.3
  • 24
    • 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
  • 26
    • 0024315260 scopus 로고
    • The mechanism of biotin-dependent enzymes
    • Knowles, J. R. (1989) The mechanism of biotin-dependent enzymes, Annu. Rev. Biochem. 58, 195-221.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 195-221
    • Knowles, J.R.1
  • 27
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures, J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 28
    • 0001453814 scopus 로고
    • The Enzymatic Synthesis of Holotranscarboxylase from Apotranscarboxylase and (+)-Biotin
    • Lane, M. D., Rominger, K. L., Young, D. L., & Lynen, F. (1964) The Enzymatic Synthesis of Holotranscarboxylase from Apotranscarboxylase and (+)-Biotin, J. Biol. Chem. 239, 2865-2871.
    • (1964) J. Biol. Chem. , vol.239 , pp. 2865-2871
    • Lane, M.D.1    Rominger, K.L.2    Young, D.L.3    Lynen, F.4
  • 29
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. W. (1993) PROCHECK: a program to check the stereochemical quality of protein structures, J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.W.4
  • 30
    • 0029064585 scopus 로고
    • Isolation of a cDNa Encoding Human Holocarboxylase Synthetase by Functional Complementation of a Biotin Auxotroph of Escherichia coli
    • Leon-Del-Rio, A., Leclerc, D., Akerman, B., Wakamatsu, N., & Gravel, R. A. (1995) Isolation of a cDNA Encoding Human Holocarboxylase Synthetase by Functional Complementation of a Biotin Auxotroph of Escherichia coli, Proc. Natl. Acad. Sci. U.S.A. 92, 4226-4230.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 4226-4230
    • Leon-Del-Rio, A.1    Leclerc, D.2    Akerman, B.3    Wakamatsu, N.4    Gravel, R.A.5
  • 31
    • 0026502763 scopus 로고
    • The Gene Encoding the Biotin Carboxylase Subunit of Escherichia coli Acetyl-CoA Carboxylase
    • Li, S.-J., & Cronan, J. E., Jr. (1992a) The Gene Encoding the Biotin Carboxylase Subunit of Escherichia coli Acetyl-CoA Carboxylase, J. Biol. Chem. 267, 855-863.
    • (1992) J. Biol. Chem. , vol.267 , pp. 855-863
    • Li, S.-J.1    Cronan J.E., Jr.2
  • 32
    • 0026787447 scopus 로고
    • The Genes Encoding the Two Carboxyltransferase Subunits of Escherichia coli Acetyl-CoA Carboxylase
    • Li, S.-J., & Cronan, J. E., Jr. (1992b) The Genes Encoding the Two Carboxyltransferase Subunits of Escherichia coli Acetyl-CoA Carboxylase, J. Biol. Chem. 267, 16841-16847.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16841-16847
    • Li, S.-J.1    Cronan J.E., Jr.2
  • 33
    • 0023758327 scopus 로고
    • Sequence and Domain Structure of Yeast Pyruvate Carboxylase
    • Lim, F., Morris, C. P., Occhiodoro, F., & Wallace, J. C. (1988) Sequence and Domain Structure of Yeast Pyruvate Carboxylase, J. Biol. Chem. 263, 11493-11497.
    • (1988) J. Biol. Chem. , vol.263 , pp. 11493-11497
    • Lim, F.1    Morris, C.P.2    Occhiodoro, F.3    Wallace, J.C.4
  • 34
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity
    • Lipari, G., & Szabo, A. (1982) Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity, J. Am. Chem. Soc. 104, 4546-4559.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 35
    • 0028941877 scopus 로고
    • Backbone dynamics of Escherichia coli Ribonuclease HI: Correlations with structure and function in an active enzyme
    • Mandel, A. M., Mikael, A., & Palmer, 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    Mikael, A.2    Palmer, A.G.3
  • 36
    • 0000144365 scopus 로고
    • Baseline correction of 2D FT NMR spectra using a simple linear prediction extrapolation of the time-domain data
    • Marion, D., & Bax, A. (1989) Baseline correction of 2D FT NMR spectra using a simple linear prediction extrapolation of the time-domain data, J. Magn. Reson. 83, 205-211.
    • (1989) J. Magn. Reson. , vol.83 , pp. 205-211
    • Marion, D.1    Bax, A.2
  • 39
    • 45249127991 scopus 로고
    • Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins
    • Marion, D., Ikura, M., Tschudin, R., & Bax, A. (1989c) Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins, J. Magn. Reson. 85, 393-399.
    • (1989) J. Magn. Reson. , vol.85 , pp. 393-399
    • Marion, D.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 40
    • 0002899752 scopus 로고
    • Modified spin-echo method for measuring nuclear spin relaxation times
    • Meiboom, S., & Gill, D. (1958) Modified spin-echo method for measuring nuclear spin relaxation times, Rev. Sci. Instrum. 29, 688-691.
    • (1958) Rev. Sci. Instrum. , vol.29 , pp. 688-691
    • Meiboom, S.1    Gill, D.2
  • 41
    • 0029986466 scopus 로고    scopus 로고
    • Purification and characterization of intact and truncated forms of the Escherichia coli biotin carboxyl carrier subunit of acetyl-CoA carboxylase
    • Nenortas, E., & Beckett, D. (1996) Purification and characterization of intact and truncated forms of the Escherichia coli biotin carboxyl carrier subunit of acetyl-CoA carboxylase. J. Biol. Chem. 271, 7559-7567.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7559-7567
    • Nenortas, E.1    Beckett, D.2
  • 44
    • 0027975343 scopus 로고
    • X-ray Structure Determination at 2.6-Å Resolution of a Lipoate-Containing Protein: The H-protein of the Glycine Decarboxylase Complex from Pea Leaves
    • Pares, S., Cohen-Addad, C., Sieker, L., Neuburger, M., & Douce, R. (1994) X-ray Structure Determination at 2.6-Å Resolution of a Lipoate-Containing Protein: The H-protein of the Glycine Decarboxylase Complex from Pea Leaves. Proc. Natl. Acad. Sci. U.S.A. 91, 4850-4853.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 4850-4853
    • Pares, S.1    Cohen-Addad, C.2    Sieker, L.3    Neuburger, M.4    Douce, R.5
  • 45
    • 0000660936 scopus 로고
    • Mapping of spectral density functions using heteronuclear NMR relaxation measurements
    • Peng, J. W., & Wagner, G. (1992) Mapping of spectral density functions using heteronuclear NMR relaxation measurements. J. Magn. Reson. 98, 308-332.
    • (1992) J. Magn. Reson. , vol.98 , pp. 308-332
    • Peng, J.W.1    Wagner, G.2
  • 46
    • 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
  • 50
    • 48749144559 scopus 로고
    • Evaluation of a new broadband decoupling sequence: WALTZ-16
    • Shaka, A. J., Keler, J., & Freeman, R. (1983) Evaluation of a new broadband decoupling sequence: WALTZ-16, J. Magn. Reson. 53, 313-340.
    • (1983) J. Magn. Reson. , vol.53 , pp. 313-340
    • Shaka, A.J.1    Keler, J.2    Freeman, R.3
  • 51
    • 0026192276 scopus 로고
    • Measurement of the exchange rates of rapidly exchanging amide protons: Application to the study of calmodulin and its complex with myosin light chain kinase fragment
    • Spera, S., Ikura, M., & Bax, A. (1991) Measurement of the exchange rates of rapidly exchanging amide protons: application to the study of calmodulin and its complex with myosin light chain kinase fragment, J. Biomol. NMR 1, 155-165.
    • (1991) J. Biomol. NMR , vol.1 , pp. 155-165
    • Spera, S.1    Ikura, M.2    Bax, A.3
  • 54
    • 36849104960 scopus 로고
    • Measurement of spin relaxation in complex systems
    • Vold, R. L., Waugh, J. S., Klein, M. P., & Phelps, D. E. (1968) Measurement of spin relaxation in complex systems, J. Chem. Phys. 48, 3831-3832.
    • (1968) J. Chem. Phys. , vol.48 , pp. 3831-3832
    • Vold, R.L.1    Waugh, J.S.2    Klein, M.P.3    Phelps, D.E.4
  • 55
    • 0028085434 scopus 로고
    • Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase
    • Waldrop, G. L., Rayment, I., & Holden, H. M. (1994) Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase, Biochemistry 33, 10249-10256.
    • (1994) Biochemistry , vol.33 , pp. 10249-10256
    • Waldrop, G.L.1    Rayment, I.2    Holden, H.M.3
  • 56
    • 0026666377 scopus 로고
    • Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin and DNA binding domains
    • Wilson, K. P., Shewchuk, L. M., Brennan, R. G., Otsuka, A. J., & Matthews, B. W. (1992) Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin and DNA binding domains, Proc. Natl. Acad. Sci. U.S.A. 89, 9257-9261.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 9257-9261
    • Wilson, K.P.1    Shewchuk, L.M.2    Brennan, R.G.3    Otsuka, A.J.4    Matthews, B.W.5
  • 57
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • Wishart, D. S., Sykes, B. D., & Richards, F. M. (1991) Relationship between nuclear magnetic resonance chemical shift and protein secondary structure, J. Mol. Biol. 222, 311-333.
    • (1991) J. Mol. Biol. , vol.222 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 58
    • 0026597879 scopus 로고
    • The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
    • Wishart, D. S., Sykes, B. D., & Richards, F. M. (1992) The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31, 1647-1651.
    • (1992) Biochemistry , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 60
    • 0028541866 scopus 로고
    • 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques
    • 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques, J. Biomol. NMR 4, 845-858.
    • (1994) J. Biomol. NMR , vol.4 , pp. 845-858
    • Zhang, O.1    Kay, L.E.2    Olivier, J.P.3    Forman-Kay, J.D.4
  • 61
    • 0001076476 scopus 로고
    • Discrete Fourier transformation of NMR signals. the relationship between sampling delay time and spectral baseline
    • Zhu, G., Torchia, D. A., & Bax, A. (1993) Discrete Fourier transformation of NMR signals. The relationship between sampling delay time and spectral baseline, J. Magn. Reson., Ser. A 105, 219-222.
    • (1993) J. Magn. Reson., Ser. A , vol.105 , pp. 219-222
    • Zhu, G.1    Torchia, D.A.2    Bax, A.3


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