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Volumn 25, Issue , 1996, Pages 163-195

Use of 19F NMR to probe protein structure and conformational changes

Author keywords

Dynamics; Fluorine; Paramagnetic broadening; Spin label; X ray crystallography

Indexed keywords

AMINO ACID RECEPTOR; ASPARTATE RECEPTOR; BACTERIAL PROTEIN; CALCIUM BINDING PROTEIN; CARRIER PROTEIN; DIHYDROFOLATE REDUCTASE; FLUORINE; GALACTOSE-BINDING PROTEIN; GALAPTIN; GLUCOSE TRANSPORTER; LACTATE DEHYDROGENASE; MEMBRANE PROTEIN; METHYL ACCEPTING CHEMOTAXIS PROTEINS; METHYL-ACCEPTING CHEMOTAXIS PROTEINS; PERIPLASMIC BINDING PROTEIN; SOLVENT; ASPARTIC ACID; ELONGATION FACTOR TU; FLUORIDE; LACTOSE; OXIDOREDUCTASE;

EID: 0029665619     PISSN: 10568700     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.bb.25.060196.001115     Document Type: Article
Times cited : (296)

References (100)
  • 1
    • 0025094671 scopus 로고
    • Enzyme inhibition by fluoro compounds
    • Abeles RH, Alston TA. 1990. Enzyme inhibition by fluoro compounds. J. Biol. Chem. 265:16705-8
    • (1990) J. Biol. Chem. , vol.265 , pp. 16705-16708
    • Abeles, R.H.1    Alston, T.A.2
  • 4
    • 0028244638 scopus 로고
    • Magnesium binding to the bacterial chemotaxis protein CheY results in large conformational changes involving its functional surface
    • Bellsolell L, Prieto J, Serrano L, Coll M. 1994. Magnesium binding to the bacterial chemotaxis protein CheY results in large conformational changes involving its functional surface. J. Mol, Biol. 238:489-95
    • (1994) J. Mol, Biol. , vol.238 , pp. 489-495
    • Bellsolell, L.1    Prieto, J.2    Serrano, L.3    Coll, M.4
  • 5
    • 0028089151 scopus 로고
    • Aspartate receptors of Escherichia coli and Salmonella typhimurium bind ligand with negative and half-of-sites cooperativity
    • Biemann H-P, Koshland DE Jr. 1994. Aspartate receptors of Escherichia coli and Salmonella typhimurium bind ligand with negative and half-of-sites cooperativity. Biochemistry 33: 629-34
    • (1994) Biochemistry , vol.33 , pp. 629-634
    • Biemann, H.-P.1    Koshland Jr., D.E.2
  • 6
    • 0025908814 scopus 로고
    • Signal transduction pathways involving protein phosphorylation in prokaryotes
    • Bourret RB, Brokovich KA, Simon MI. 1991. Signal transduction pathways involving protein phosphorylation in prokaryotes. Annu. Rev. Biochem. 60:401-41
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 401-441
    • Bourret, R.B.1    Brokovich, K.A.2    Simon, M.I.3
  • 8
    • 0025883798 scopus 로고
    • Influence of polyfluorination of the phenylalanine ring of angiotensin II on conformation and biological activity
    • Bovy PR, Getman DP, Matsoukas JM, Moore GJ. 1991. Influence of polyfluorination of the phenylalanine ring of angiotensin II on conformation and biological activity. Biochim. Biophys. Acta 1079:23-28
    • (1991) Biochim. Biophys. Acta , vol.1079 , pp. 23-28
    • Bovy, P.R.1    Getman, D.P.2    Matsoukas, J.M.3    Moore, G.J.4
  • 10
    • 0025270551 scopus 로고
    • + holoenzyme and the folate NADP+ ternary complex. Substrate binding and a model for the transition state
    • + holoenzyme and the folate NADP+ ternary complex. Substrate binding and a model for the transition state. Biochemistry 29:3263-77
    • (1990) Biochemistry , vol.29 , pp. 3263-3277
    • Bystroff, C.1    Oatley, S.J.2    Kraut, J.3
  • 12
    • 0028103622 scopus 로고
    • Origins of fluorine chemical shifts in proteins
    • Chambers SE, Lau EY, Gerig JT. 1994. Origins of fluorine chemical shifts in proteins. J. Am. Chem. Soc. 116:3603-4
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 3603-3604
    • Chambers, S.E.1    Lau, E.Y.2    Gerig, J.T.3
  • 13
    • 0029865503 scopus 로고    scopus 로고
    • Molecular mechanism of transmembrane signaling by the aspartate receptor
    • In press
    • Chervitz SA, Falke JJ. 1996. Molecular mechanism of transmembrane signaling by the aspartate receptor. Proc. Natl. Acad. Sci. USA. In press
    • (1996) Proc. Natl. Acad. Sci. USA
    • Chervitz, S.A.1    Falke, J.J.2
  • 14
    • 0028818765 scopus 로고
    • Lock on/ off disulfides identify the transemembrane signaling helix of the aspartate receptor
    • Chervitz SA, Falke JJ. 1995. Lock on/ off disulfides identify the transemembrane signaling helix of the aspartate receptor. J. Biol. Chem. 41:24043-53
    • (1995) J. Biol. Chem. , vol.41 , pp. 24043-24053
    • Chervitz, S.A.1    Falke, J.J.2
  • 15
    • 0029130732 scopus 로고
    • Transmembrane signaling by the aspartate receptor: Engineered disulfides reveal static regions of the subunit interface
    • Chervitz SA, Lin CM, Falke JJ. 1995. Transmembrane signaling by the aspartate receptor: engineered disulfides reveal static regions of the subunit interface. Biochemistry 34:9722-33
    • (1995) Biochemistry , vol.34 , pp. 9722-9733
    • Chervitz, S.A.1    Lin, C.M.2    Falke, J.J.3
  • 18
    • 0027380709 scopus 로고
    • Fluorine-19 nuclear magnetic resonance studies of binary and ternary nuclear magnetic resonance studies of binary and ternary complexes of thymidilate synthase utilizing a fluorine-labeled folate analogue
    • Connick TJ, Reilly RT, Dunlap RB, Ellis PD. 1993. Fluorine-19 nuclear magnetic resonance studies of binary and ternary nuclear magnetic resonance studies of binary and ternary complexes of thymidilate synthase utilizing a fluorine-labeled folate analogue. Biochemistry 32:9888-95
    • (1993) Biochemistry , vol.32 , pp. 9888-9895
    • Connick, T.J.1    Reilly, R.T.2    Dunlap, R.B.3    Ellis, P.D.4
  • 20
    • 1542704675 scopus 로고    scopus 로고
    • Fluorine NMR of proteins involved in chemotaxis
    • ed. DM Grant, RK Harris, Chichester: Wiley
    • Danielson MA, Falke JJ. 1996. Fluorine NMR of proteins involved in chemotaxis. In Encyclopedia of Nuclear Magnetic Resonance, ed. DM Grant, RK Harris, pp. 855-61 Chichester: Wiley.
    • (1996) Encyclopedia of Nuclear Magnetic Resonance , pp. 855-861
    • Danielson, M.A.1    Falke, J.J.2
  • 21
    • 0027308278 scopus 로고
    • Secondary and tertiary structural effects on protein NMR chemical shifts: An ab initio approach
    • de Dios AC, Pearson JG, Oldfield E. 1993. Secondary and tertiary structural effects on protein NMR chemical shifts: an ab initio approach. Science 260:1491-96
    • (1993) Science , vol.260 , pp. 1491-1496
    • De Dios, A.C.1    Pearson, J.G.2    Oldfield, E.3
  • 25
    • 0023224051 scopus 로고
    • Global flexibility in a sensory receptor: A site-directed cross-linking approach
    • Falke JJ, Koshland DE Jr. 1987. Global flexibility in a sensory receptor: a site-directed cross-linking approach. Science 237:1596-600
    • (1987) Science , vol.237 , pp. 1596-1600
    • Falke, J.J.1    Koshland Jr., D.E.2
  • 26
    • 0026612027 scopus 로고
    • 19F nuclear magnetic resonance studies of aqueous and transmembrane receptors. Examples from the Escherichia coli chemosensory pathway
    • 19F nuclear magnetic resonance studies of aqueous and transmembrane receptors. Examples from the Escherichia coli chemosensory pathway. Biophys. J. 62:82-86
    • (1992) Biophys. J. , vol.62 , pp. 82-86
    • Falke, J.J.1    Luck, L.A.2    Scherrer, J.3
  • 27
    • 0028002085 scopus 로고
    • The 1.9 Å X-ray structure of a closed unliganded form of the glucose/galactose receptor from Salmonella typhimurium
    • Flocco MM, Mobray SL. 1994. The 1.9 Å X-ray structure of a closed unliganded form of the glucose/galactose receptor from Salmonella typhimurium. J. Biol. Chem. 269:8931-36
    • (1994) J. Biol. Chem. , vol.269 , pp. 8931-8936
    • Flocco, M.M.1    Mobray, S.L.2
  • 29
    • 0015527141 scopus 로고
    • Magnetic resonance studies of protein-small molecule interactions. Binding of N-trifluoroacetyl-D-(and L-)-p-fluorophenylalanine to chymotrypsin
    • Gammon KL, Smallcombe SH, Richards JH. 1972. Magnetic resonance studies of protein-small molecule interactions. Binding of N-trifluoroacetyl-D-(and L-)-p-fluorophenylalanine to chymotrypsin. J. Am. Chem. Soc. 94:4573-80
    • (1972) J. Am. Chem. Soc. , vol.94 , pp. 4573-4580
    • Gammon, K.L.1    Smallcombe, S.H.2    Richards, J.H.3
  • 31
    • 0024850562 scopus 로고
    • Fluorine nuclear magnetic resonance of fluorinated ligands
    • Gerig JT. 1989. Fluorine nuclear magnetic resonance of fluorinated ligands. Methods Enzymol. 177:3-23
    • (1989) Methods Enzymol. , vol.177 , pp. 3-23
    • Gerig, J.T.1
  • 32
    • 0026172002 scopus 로고
    • Prediction of fluorine chemical shifts in proteins
    • Gregory DH, Gerig JT. 1991. Prediction of fluorine chemical shifts in proteins. Biopolymers 31:845-58
    • (1991) Biopolymers , vol.31 , pp. 845-858
    • Gregory, D.H.1    Gerig, J.T.2
  • 33
    • 84986492813 scopus 로고
    • Structural effects of fluorine substitution in proteins
    • Gregory DH, Gerig JT. 1991. Structural effects of fluorine substitution in proteins. J. Comp. Chem. 12:180-85
    • (1991) J. Comp. Chem. , vol.12 , pp. 180-185
    • Gregory, D.H.1    Gerig, J.T.2
  • 34
    • 0027293539 scopus 로고
    • Novel heteronuclear methods of assignment transfer from a diamagnetic to a paramagnetic protein: Application to rat cytochrome b5
    • Guiles RD, Basus VJ, Sarma S, Malpure S, Fox KM, et al. 1993. Novel heteronuclear methods of assignment transfer from a diamagnetic to a paramagnetic protein: application to rat cytochrome b5. Biochemistry 32: 8329-40
    • (1993) Biochemistry , vol.32 , pp. 8329-8340
    • Guiles, R.D.1    Basus, V.J.2    Sarma, S.3    Malpure, S.4    Fox, K.M.5
  • 35
    • 0027408328 scopus 로고
    • Bacterial motility and signal transduciton
    • Hazelbauer GL, Berg HC, Matsumura P. 1993. Bacterial motility and signal transduciton. Cell 73:15-22
    • (1993) Cell , vol.73 , pp. 15-22
    • Hazelbauer, G.L.1    Berg, H.C.2    Matsumura, P.3
  • 38
    • 0024539619 scopus 로고
    • Membrane-bound D-lactate dehydrogenase of Escherichia coli: A model for protein interactions in membranes
    • Ho C, Pratt EA, Wu C-S, Yang JT. 1989. Membrane-bound D-lactate dehydrogenase of Escherichia coli: a model for protein interactions in membranes. Biochim. Biophys. Acta 988: 173-84
    • (1989) Biochim. Biophys. Acta , vol.988 , pp. 173-184
    • Ho, C.1    Pratt, E.A.2    Wu, C.-S.3    Yang, J.T.4
  • 39
    • 0028175779 scopus 로고
    • 19F]tryptophan-labeled Escherichia coli dihydrofolate reductase: Equilibrium folding and ligand binding studies
    • 19F]tryptophan-labeled Escherichia coli dihydrofolate reductase: equilibrium folding and ligand binding studies. Biochemistry 33:5502-9
    • (1994) Biochemistry , vol.33 , pp. 5502-5509
    • Hoeltzi, S.D.1    Frieden, C.2
  • 41
    • 85011556853 scopus 로고
    • 19F NMR spectroscopy to protein folding: Studies of E. coli dihydrofolate reductase
    • 19F NMR spectroscopy to protein folding: studies of E. coli dihydrofolate reductase. Tech. Protein Chem. 5:455-65
    • (1994) Tech. Protein Chem. , vol.5 , pp. 455-465
    • Hoeltzi, S.D.1    Ropson, I.J.2    Freiden, C.3
  • 42
    • 0017224909 scopus 로고
    • Fluorine-19 nuclear magnetic resonance study of fluorotyrosine alkaline phosphatase: The influence of zinc on protein structure and a conformational change induced by phosphate binding
    • Hull WE, Sykes, BD. 1976. Fluorine-19 nuclear magnetic resonance study of fluorotyrosine alkaline phosphatase: the influence of zinc on protein structure and a conformational change induced by phosphate binding. Biochemistry 15:1535-46
    • (1976) Biochemistry , vol.15 , pp. 1535-1546
    • Hull, W.E.1    Sykes, B.D.2
  • 43
    • 1542599759 scopus 로고
    • Dynamics at the active site of N-(4-fluorophenyl),N-(2,6-difluorophenyl)carbamoyl-α-chymotrypsin
    • In press
    • Johnson CD, Gerig JT. 1995. Dynamics at the active site of N-(4-fluorophenyl),N-(2,6-difluorophenyl)carbamoyl-α-chymotrypsin. Magn. Res. Chem. In press
    • (1995) Magn. Res. Chem.
    • Johnson, C.D.1    Gerig, J.T.2
  • 44
    • 0025093242 scopus 로고
    • The specific incorporation of labelled aromatic ammo acids into proteins through growth of bacteria in the presence of glyphosate
    • Kim H-W, Perez JA, Ferguson SJ, Campbell ID. 1990. The specific incorporation of labelled aromatic ammo acids into proteins through growth of bacteria in the presence of glyphosate. FEBS Lett. 272:34-36
    • (1990) FEBS Lett. , vol.272 , pp. 34-36
    • Kim, H.-W.1    Perez, J.A.2    Ferguson, S.J.3    Campbell, I.D.4
  • 45
    • 0024093976 scopus 로고
    • Maltose chemoreceptor of Escherichia coli interaction of maltose-binding protein and the tar signal transducer
    • Kossman M, Wolff C, Manson MD. 1988. Maltose chemoreceptor of Escherichia coli interaction of maltose-binding protein and the tar signal transducer. J. Bacteriol. 170:4516-21
    • (1988) J. Bacteriol. , vol.170 , pp. 4516-4521
    • Kossman, M.1    Wolff, C.2    Manson, M.D.3
  • 47
    • 0025855955 scopus 로고
    • Direct electrophilic fluorination of tyrosine in dermorphin analogs and its effect on biological activity, receptor affinity, and selectivity
    • Labroo VM, Hebel D, Krik KL, Cohen LA, Lemieux C, Schiller PW. 1991. Direct electrophilic fluorination of tyrosine in dermorphin analogs and its effect on biological activity, receptor affinity, and selectivity. Int. J. Pept. Protein Res. 37:440-49
    • (1991) Int. J. Pept. Protein Res. , vol.37 , pp. 440-449
    • Labroo, V.M.1    Hebel, D.2    Krik, K.L.3    Cohen, L.A.4    Lemieux, C.5    Schiller, P.W.6
  • 48
    • 0029047850 scopus 로고
    • Identification of functionally important helical faces in transmembrane segments by scanning mutagenesis
    • Lee GF, Dutton DP, Hazelbauer GL. 1995. Identification of functionally important helical faces in transmembrane segments by scanning mutagenesis. Proc. Natl. Acad. Sci. USA 92: 5416-20
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5416-5420
    • Lee, G.F.1    Dutton, D.P.2    Hazelbauer, G.L.3
  • 49
    • 0024412948 scopus 로고
    • Nuclear magnetic resonance studies of 6-fluorotryptophan-substituted rat cellular retinol-pinding protein II produced in Escherichia coli
    • Li E, Qian S-J, Nader L, Young N-CC, d'Avignon A, et al. 1989. Nuclear magnetic resonance studies of 6-fluorotryptophan-substituted rat cellular retinol-pinding protein II produced in Escherichia coli. J. Biol. Chem. 264: 17041-48
    • (1989) J. Biol. Chem. , vol.264 , pp. 17041-17048
    • Li, E.1    Qian, S.-J.2    Nader, L.3    Young, N.-C.C.4    D'Avignon, A.5
  • 50
    • 0025194826 scopus 로고
    • Nuclear magnetic resonance studies of 6-fluorotryptophan-substituted rat cellular retinol binding protein II produced in Escherichia coli
    • Li E, Quian S-J, Yang N-CC, d'Avignon A, Gordon JI. 1990. Nuclear magnetic resonance studies of 6-fluorotryptophan-substituted rat cellular retinol binding protein II produced in Escherichia coli. J. Biol. Chem. 265: 11549-54
    • (1990) J. Biol. Chem. , vol.265 , pp. 11549-11554
    • Li, E.1    Quian, S.-J.2    Yang, N.-C.C.3    D'Avignon, A.4    Gordon, J.I.5
  • 51
    • 0028216598 scopus 로고
    • Fluoine-19 nuclear magnetic resonance spectroscopic study of fluorophenylalanine-and flurortryptophan-labeled avian egg white lysozymes
    • Lian C, Le H, Montez B, Patterson J, Harrell S, et al. 1994. Fluoine-19 nuclear magnetic resonance spectroscopic study of fluorophenylalanine-and flurortryptophan-labeled avian egg white lysozymes. Biochemistry 33:5238-45
    • (1994) Biochemistry , vol.33 , pp. 5238-5245
    • Lian, C.1    Le, H.2    Montez, B.3    Patterson, J.4    Harrell, S.5
  • 52
    • 0028099669 scopus 로고
    • Signal transduction in chemotaxis. A propogating conformation change upon phosphorylation of cheY
    • Lowry DF, Roth AF, Rupert AF, Rupert PB, Dahlquist FW, et al. 1994. Signal transduction in chemotaxis. A propogating conformation change upon phosphorylation of cheY. J. Biol. Chem. 269:26358-62
    • (1994) J. Biol. Chem. , vol.269 , pp. 26358-26362
    • Lowry, D.F.1    Roth, A.F.2    Rupert, A.F.3    Rupert, P.B.4    Dahlquist, F.W.5
  • 53
    • 0344277044 scopus 로고
    • Lac repressor: 3-fluorotyrosine substitution for nuclear magnetic resonance studies
    • Lu P, Jarema M, Mosser K, Daniel WE. 1976. Lac repressor: 3-fluorotyrosine substitution for nuclear magnetic resonance studies. Proc. Natl. Acad. Sci. USA 73:3471-75
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 3471-3475
    • Lu, P.1    Jarema, M.2    Mosser, K.3    Daniel, W.E.4
  • 54
    • 0025922013 scopus 로고
    • 19F NMR studies of the D-galactose chemosensory receptor. 1. Sugar binding yields a global structural change
    • 19F NMR studies of the D-galactose chemosensory receptor. 1. Sugar binding yields a global structural change. Biochemistry 30:4248-56
    • (1991) Biochemistry , vol.30 , pp. 4248-4256
    • Luck, L.A.1    Falke, J.J.2
  • 55
    • 0025922014 scopus 로고
    • 19F NMR studies of the D-galactose chemosensory receptor. 2. Ca(II) Binding yields a local structural change
    • 19F NMR studies of the D-galactose chemosensory receptor. 2. Ca(II) Binding yields a local structural change. Biochemistry 30:4257-61
    • (1991) Biochemistry , vol.30 , pp. 4257-4261
    • Luck, L.A.1    Falke, J.J.2
  • 56
    • 0025821340 scopus 로고
    • 19F NMR studies of cleft angle in the D-galactose chemosensory receptor
    • 19F NMR studies of cleft angle in the D-galactose chemosensory receptor. Biochemistry 30:6484-90
    • (1991) Biochemistry , vol.30 , pp. 6484-6490
    • Luck, L.A.1    Falke, J.J.2
  • 57
    • 0026512864 scopus 로고
    • Phosphorylation of bacterial response regulator proteins by low molecular weight phospho-donors
    • Lukat GS, McCleary WR, Stock AM, Stock JB. 1992. Phosphorylation of bacterial response regulator proteins by low molecular weight phospho-donors. Proc. Natl. Acat. Sci. USA 89: 718-22
    • (1992) Proc. Natl. Acat. Sci. USA , vol.89 , pp. 718-722
    • Lukat, G.S.1    McCleary, W.R.2    Stock, A.M.3    Stock, J.B.4
  • 58
    • 0020478556 scopus 로고
    • Hinge-bending in L-arabinose binding protein: The "venus-flytrap" model
    • Mao B, Pear MR, McCammon JA, Quiocho FA. 1982. Hinge-bending in L-arabinose binding protein: the "venus-flytrap" model J. Biol. Chem. 257:1131-33
    • (1982) J. Biol. Chem. , vol.257 , pp. 1131-1133
    • Mao, B.1    Pear, M.R.2    McCammon, J.A.3    Quiocho, F.A.4
  • 60
    • 0026315513 scopus 로고
    • Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand
    • Milburn MV, Prive GG, Milligan DL, Scott WG, Yeh J, et al. 1991. Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand. Science 254:1342-47
    • (1991) Science , vol.254 , pp. 1342-1347
    • Milburn, M.V.1    Prive, G.G.2    Milligan, D.L.3    Scott, W.G.4    Yeh, J.5
  • 61
    • 0018948077 scopus 로고
    • The mechanism of sugar binding to the periplasmic receptor for galactose chemotaxis and transport in Escherichia coli
    • Miller DM, Olson JS, Quiocho FA. 1980. The mechanism of sugar binding to the periplasmic receptor for galactose chemotaxis and transport in Escherichia coli. J. Biol. Chem. 255: 2465-71
    • (1980) J. Biol. Chem. , vol.255 , pp. 2465-2471
    • Miller, D.M.1    Olson, J.S.2    Quiocho, F.A.3
  • 62
    • 0015503917 scopus 로고
    • An NMR method for characterizing conformation changes in proteins
    • Millet F, Raftery MA. 1972. An NMR method for characterizing conformation changes in proteins. Biochem. Biophys. Res. Commun. 47:625-32
    • (1972) Biochem. Biophys. Res. Commun. , vol.47 , pp. 625-632
    • Millet, F.1    Raftery, M.A.2
  • 63
    • 0023917333 scopus 로고
    • Site-directed crosslinking. Establishing the dimeric structure of the aspartate receptor of bacterial chemotaxis
    • Milligan DL, Koshland DE Jr. 1988. Site-directed crosslinking. Establishing the dimeric structure of the aspartate receptor of bacterial chemotaxis. J. Biol. Chem. 263:6268-75
    • (1988) J. Biol. Chem. , vol.263 , pp. 6268-6275
    • Milligan, D.L.1    Koshland Jr., D.E.2
  • 64
    • 0027248998 scopus 로고
    • Purification and characterization of hte periplasmic domain of the aspartate chemoreceptor
    • Milligan DL, Koshland DE Jr. 1993. Purification and characterization of hte periplasmic domain of the aspartate chemoreceptor. J. Biol. Chem. 268:19991-97
    • (1993) J. Biol. Chem. , vol.268 , pp. 19991-19997
    • Milligan, D.L.1    Koshland Jr., D.E.2
  • 65
    • 0026046559 scopus 로고
    • Disposition of the phenylalanine-B25 side-chain during insulin-receptor and insulin-insulin interactions
    • Mirmira RG, Tager HS. 1991. Disposition of the phenylalanine-B25 side-chain during insulin-receptor and insulin-insulin interactions. Biochemistry 30:8222-29
    • (1991) Biochemistry , vol.30 , pp. 8222-8229
    • Mirmira, R.G.1    Tager, H.S.2
  • 66
    • 0028026855 scopus 로고
    • Assignments, secondary structure, global fold, and dynamics of chemotaxis Y protein using three- and four-dimensional heteronuclear (13C, 15N) NMR spectroscopy
    • Moy FJ, Lowry DF, Matsumura P, Dahlquist FW, Krywko JE, Domaille PJ. 1994. Assignments, secondary structure, global fold, and dynamics of chemotaxis Y protein using three- and four-dimensional heteronuclear (13C, 15N) NMR spectroscopy. Biochemistry 33:10131-42
    • (1994) Biochemistry , vol.33 , pp. 10131-10142
    • Moy, F.J.1    Lowry, D.F.2    Matsumura, P.3    Dahlquist, F.W.4    Krywko, J.E.5    Domaille, P.J.6
  • 67
    • 0004524514 scopus 로고
    • Intermolecular interactions of the C-F bond: The crystallographic environment of fluorinated carboxylic acids and related structures
    • Murray-Rust P, Stallings WC, Monti CT, Preston RK, Glusker JP. 1983. Intermolecular interactions of the C-F bond: the crystallographic environment of fluorinated carboxylic acids and related structures. J. Am. Chem. Soc. 105:3206-14
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 3206-3214
    • Murray-Rust, P.1    Stallings, W.C.2    Monti, C.T.3    Preston, R.K.4    Glusker, J.P.5
  • 68
    • 0027056677 scopus 로고
    • Communication modules in bacterial signaling proteins
    • Parkinson JS, Kofoid EC. 1992. Communication modules in bacterial signaling proteins. Annu. Rev. Genet. 26: 71-112
    • (1992) Annu. Rev. Genet. , vol.26 , pp. 71-112
    • Parkinson, J.S.1    Kofoid, E.C.2
  • 70
    • 0001465616 scopus 로고
    • Chemical shifts in proteins: A shielding trajectory analysis of the fluorine nuclear magnetic resonance spectrum of the Escherichia coli galactose binding protein using a multipole shielding polarizability-local reaction field-molecular dynamics approach
    • Pearson JG, Oldfield E, Lee FS, Warshell A. 1993. Chemical shifts in proteins: a shielding trajectory analysis of the fluorine nuclear magnetic resonance spectrum of the Escherichia coli galactose binding protein using a multipole shielding polarizability-local reaction field-molecular dynamics approach. J. Am. Chem. Soc. 115: 6851-62
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 6851-6862
    • Pearson, J.G.1    Oldfield, E.2    Lee, F.S.3    Warshell, A.4
  • 72
    • 0021684863 scopus 로고
    • Fluorine-19 nuclear magnetic resonance study of 5-fluorotryptophan-labeled histidine-binding protein J of Salmonella typhimurium
    • Post JF, Cottam PF, Simplaceanu V, Ho C. 1984. Fluorine-19 nuclear magnetic resonance study of 5-fluorotryptophan-labeled histidine-binding protein J of Salmonella typhimurium. J. Mol. Biol. 179:729-43
    • (1984) J. Mol. Biol. , vol.179 , pp. 729-743
    • Post, J.F.1    Cottam, P.F.2    Simplaceanu, V.3    Ho, C.4
  • 73
    • 0016713512 scopus 로고
    • Incorporation of fluorotryptophans into proteins of Escherichia coli
    • Pratt EA, Ho C. 1975. Incorporation of fluorotryptophans into proteins of Escherichia coli. Biochemistry 14: 3035-40
    • (1975) Biochemistry , vol.14 , pp. 3035-3040
    • Pratt, E.A.1    Ho, C.2
  • 74
    • 0027501116 scopus 로고
    • Origin of the asymmetrical contact between lac repressor and lac operator DNA
    • Rastinejad F, Artz P, Lu P. 1993. Origin of the asymmetrical contact between lac repressor and lac operator DNA. J. Mol Biol. 233:389-99
    • (1993) J. Mol Biol. , vol.233 , pp. 389-399
    • Rastinejad, F.1    Artz, P.2    Lu, P.3
  • 76
    • 0027283895 scopus 로고
    • 19F nuclear magnetic resonance observations at 5-fluorouracil-substituted promotor DNA and RNA transcript
    • 19F nuclear magnetic resonance observations at 5-fluorouracil-substituted promotor DNA and RNA transcript. J. Mol. Biol. 232:105-22
    • (1993) J. Mol. Biol. , vol.232 , pp. 105-122
    • Rastinejad, F.1    Lu, P.2
  • 78
    • 0023151850 scopus 로고
    • Nuclear magnetic resonance and molecular genetic studies of the membrane-bound D-lactate dehydrogenase of Escherichia coli
    • Rule GS, Pratt EA, Simplaceanu V, Ho C. 1987. Nuclear magnetic resonance and molecular genetic studies of the membrane-bound D-lactate dehydrogenase of Escherichia coli. Biochemistry 26:549-56
    • (1987) Biochemistry , vol.26 , pp. 549-556
    • Rule, G.S.1    Pratt, E.A.2    Simplaceanu, V.3    Ho, C.4
  • 79
    • 0019953987 scopus 로고
    • Signal processing times in bacterial chemotaxis
    • Segall JE, Manson MD, Berg HC. 1982. Signal processing times in bacterial chemotaxis. Nature 296:855-57
    • (1982) Nature , vol.296 , pp. 855-857
    • Segall, J.E.1    Manson, M.D.2    Berg, H.C.3
  • 80
    • 0026493924 scopus 로고
    • Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis
    • Sharff AJ, Rodseth LE, Spurlino JC, Quiocho FA. 1992 Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis. Biochemistry 31: 10657-63
    • (1992) Biochemistry , vol.31 , pp. 10657-10663
    • Sharff, A.J.1    Rodseth, L.E.2    Spurlino, J.C.3    Quiocho, F.A.4
  • 81
    • 0014201796 scopus 로고
    • Enzyme-substrate interaction by nuclear magnetic resonance
    • Spotswood TM, Evans JM. Richards JH. 1967. Enzyme-substrate interaction by nuclear magnetic resonance. J. Am. Chem. Soc. 89:5052-54
    • (1967) J. Am. Chem. Soc. , vol.89 , pp. 5052-5054
    • Spotswood, T.M.1    Evans, J.M.2    Richards, J.H.3
  • 82
    • 0027338597 scopus 로고
    • 19F NMR titration of phosphorylase molecules binding to fluorine-labeled glycogen particles
    • 19F NMR titration of phosphorylase molecules binding to fluorine-labeled glycogen particles. Carbohydr. Res. 249:253-58
    • (1993) Carbohydr. Res. , vol.249 , pp. 253-258
    • Stirtan, W.1    Withers, S.G.2
  • 84
    • 0025805549 scopus 로고
    • Bacterial chemotaxis and the molecular logic of intracellular signal transduction networks
    • Stock JB, Lukat GS. 1991. Bacterial chemotaxis and the molecular logic of intracellular signal transduction networks. Annu. Rev. Biophys. Biophys. Chem. 20:109-36
    • (1991) Annu. Rev. Biophys. Biophys. Chem. , vol.20 , pp. 109-136
    • Stock, J.B.1    Lukat, G.S.2
  • 87
    • 0017908546 scopus 로고
    • Fluorine nuclear magnetic resonance studies of proteins
    • Sykes BD, Hull, WE. 1978. Fluorine nuclear magnetic resonance studies of proteins. Methods Enzymol. 49: 270-95
    • (1978) Methods Enzymol. , vol.49 , pp. 270-295
    • Sykes, B.D.1    Hull, W.E.2
  • 88
    • 0027253252 scopus 로고
    • NMR studies of the a-chymotrypsin-〉-1-acetamido-2-(4-fluorophenyl)ethane-1-boronic acid complex
    • Sylvia LA, Gerig JT. 1993. NMR studies of the a-chymotrypsin-〉-1-acetamido-2-(4-fluorophenyl)ethane-1-boronic acid complex. Biochim. Biophys Acta 1163:321-34
    • (1993) Biochim. Biophys Acta , vol.1163 , pp. 321-334
    • Sylvia, L.A.1    Gerig, J.T.2
  • 90
    • 0022375017 scopus 로고
    • Crystallographic structure of an active, sequence-engineered ribonuclease
    • Taylor HC, Komoriya A, Chaiken IM. 1985. Crystallographic structure of an active, sequence-engineered ribonuclease. Proc. Natl. Acad. Sci. USA 82:6423-26
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 6423-6426
    • Taylor, H.C.1    Komoriya, A.2    Chaiken, I.M.3
  • 92
    • 0025732372 scopus 로고
    • Interaction of the membrane-bound D-lactate dehydrogenase of Escherichia coli with phospholipid vesicles and reconstitution of activity using a spin-labeled fatty acid as an electron acceptor: A magnetic resonance and biochemical study
    • Truong T-TN, Pratt EA, Ho C. 1991. Interaction of the membrane-bound D-lactate dehydrogenase of Escherichia coli with phospholipid vesicles and reconstitution of activity using a spin-labeled fatty acid as an electron acceptor: a magnetic resonance and biochemical study. Biochemistry 30: 3893-98
    • (1991) Biochemistry , vol.30 , pp. 3893-3898
    • Truong, T.-T.N.1    Pratt, E.A.2    Ho, C.3
  • 94
    • 0025741662 scopus 로고
    • Crystal structure of Escherichia coli CheY refined at 1.7 Å resolution
    • Volz K, Matsumura P. 1991. Crystal structure of Escherichia coli CheY refined at 1.7 Å resolution. J. Biol. Chem. 266:15511-19
    • (1991) J. Biol. Chem. , vol.266 , pp. 15511-15519
    • Volz, K.1    Matsumura, P.2
  • 95
    • 0023256886 scopus 로고
    • A novel calcium binding site in the galactose-binding protein of bacterial transport and chemotaxis
    • Vyas NK, Vyas MN, Quiocho FA. 1987. A novel calcium binding site in the galactose-binding protein of bacterial transport and chemotaxis. Nature 327:635-38
    • (1987) Nature , vol.327 , pp. 635-638
    • Vyas, N.K.1    Vyas, M.N.2    Quiocho, F.A.3
  • 96
    • 0022555889 scopus 로고
    • Observation of internal motility of proteins by nuclear magnetic resonance in solution
    • Wagner G, Wütrich K. 1986. Observation of internal motility of proteins by nuclear magnetic resonance in solution. Methods Enzymol. 131:307-26
    • (1986) Methods Enzymol. , vol.131 , pp. 307-326
    • Wagner, G.1    Wütrich, K.2
  • 97
    • 0003820818 scopus 로고
    • The incorporation of p-fluorophenylalanine into some rabbit enzymes and other proteins
    • Westhead EW, Boyer PD. 1961. The incorporation of p-fluorophenylalanine into some rabbit enzymes and other proteins. Biochim. Biophys. Acta 54:145-50
    • (1961) Biochim. Biophys. Acta , vol.54 , pp. 145-150
    • Westhead, E.W.1    Boyer, P.D.2
  • 98
    • 0027254123 scopus 로고
    • 19F NMR studies of fluorine-labeled yeast phosphoglycerate kinase in vivo
    • 19F NMR studies of fluorine-labeled yeast phosphoglycerate kinase in vivo. Biochemistry 32:4895-902
    • (1993) Biochemistry , vol.32 , pp. 4895-4902
    • Williams, S.-P.1    Fulton, A.M.2    Brindle, K.M.3
  • 99
    • 0021814407 scopus 로고
    • Membrane protein conformational change dependent on the hydrophobic environment
    • Wilson ML, Dahlquist FW. 1985. Membrane protein conformational change dependent on the hydrophobic environment. Biochemistry 24: 1920-28
    • (1985) Biochemistry , vol.24 , pp. 1920-1928
    • Wilson, M.L.1    Dahlquist, F.W.2
  • 100
    • 0000942967 scopus 로고
    • Semisynthesis of bipyridyl-alanine cytochrome c mutants: Novel proteins with enhanced electron-transfer properties
    • Wuttke DS, Gray HB, Fisher SL, Imperaili B. 1993. Semisynthesis of bipyridyl-alanine cytochrome c mutants: novel proteins with enhanced electron-transfer properties. J. Am. Chem. Soc. 115:8455-56
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 8455-8456
    • Wuttke, D.S.1    Gray, H.B.2    Fisher, S.L.3    Imperaili, B.4


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