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Volumn 51, Issue 3, 2011, Pages 379-394

Structure, dynamics, and ionization equilibria of the tyrosine residues in Bacillus circulans xylanase

Author keywords

Glycoside hydrolase; NMR spectroscopy; Protein dynamics; Protein electrostatics; Tyrosine hydroxyl

Indexed keywords

CARBON 13; DEUTERIUM; HYDROGEN; NITROGEN 15; PROTON; TYROSINE; XYLAN ENDO 1,3 BETA XYLOSIDASE;

EID: 80755140499     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-011-9564-7     Document Type: Article
Times cited : (22)

References (82)
  • 1
    • 18144400611 scopus 로고    scopus 로고
    • Insights into the structure and function of redox-active tyrosines from model compounds
    • DOI 10.1021/jp044749y
    • BA Barry O Einarsdottir 2005 Insights into the structure and function of redox-active tyrosines from model compounds J Phys Chem B 109 6972 6981 10.1021/jp044749y (Pubitemid 40609828)
    • (2005) Journal of Physical Chemistry B , vol.109 , Issue.15 , pp. 6972-6981
    • Barry, B.A.1    Einarsdottir, O.2
  • 2
    • 0345311216 scopus 로고
    • Proton and carbon-13 assignments from sensitivity-enhanced detection of heteronuclear multiple-bond connectivity by 2D multiple quantum NMR
    • 10.1021/ja00268a061
    • A Bax MF Summers 1986 Proton and carbon-13 assignments from sensitivity-enhanced detection of heteronuclear multiple-bond connectivity by 2D multiple quantum NMR J Am Chem Soc 108 2093 2094 10.1021/ja00268a061
    • (1986) J Am Chem Soc , vol.108 , pp. 2093-2094
    • Bax, A.1    Summers, M.F.2
  • 4
    • 84985733652 scopus 로고
    • 1H-NMR parameters of the common amino-acid residues measured in aqueous-solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH
    • 10.1002/bip.1979.360180206
    • 1H-NMR parameters of the common amino-acid residues measured in aqueous-solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH Biopolymers 18 285 297 10.1002/bip.1979.360180206
    • (1979) Biopolymers , vol.18 , pp. 285-297
    • Bundi, A.1    Wüthrich, K.2
  • 5
    • 84886628398 scopus 로고
    • Temperature-dependent molecular-motion of a tyrosine residue of ferrocytochrome-C
    • 10.1016/0014-5793(76)80734-X
    • ID Campbell CM Dobson GR Moore SJ Perkins RJP Williams 1976 Temperature-dependent molecular-motion of a tyrosine residue of ferrocytochrome-C FEBS Lett 70 96 100 10.1016/0014-5793(76)80734-X
    • (1976) FEBS Lett , vol.70 , pp. 96-100
    • Campbell, I.D.1    Dobson, C.M.2    Moore, G.R.3    Perkins, S.J.4    Williams, R.J.P.5
  • 8
    • 0024594263 scopus 로고
    • Hydrogen-1 nuclear magnetic resonance studies of staphylococcal nuclease variant H124L: pH dependence of histidines and tyrosines
    • DOI 10.1016/0003-9861(89)90014-3
    • M Chinami M Shingu 1989 Hydrogen-1 nuclear magnetic resonance studies of staphylococcal nuclease variant H124L: pH-dependence of histidines and tyrosines Arch Biochem Biophys 270 126 136 10.1016/0003-9861(89)90014-3 (Pubitemid 19096139)
    • (1989) Archives of Biochemistry and Biophysics , vol.270 , Issue.1 , pp. 126-136
    • Chinami, M.1    Shingu, M.2
  • 9
    • 0032539528 scopus 로고    scopus 로고
    • Characterization of a buried neutral histidine in Bacillus circulans xylanase: Internal dynamics and interaction with a bound water molecule
    • DOI 10.1021/bi972085v
    • GP Connelly LP McIntosh 1998 Characterization of a buried neutral histidine in Bacillus circulans xylanase: internal dynamics and interaction with a bound water molecule Biochemistry 37 1810 1818 10.1021/bi972085v (Pubitemid 28099803)
    • (1998) Biochemistry , vol.37 , Issue.7 , pp. 1810-1818
    • Connelly, G.P.1    McIntosh, L.P.2
  • 10
    • 0034021175 scopus 로고    scopus 로고
    • Analysis of the dynamic properties of Bacillus circulans xylanase upon formation of a covalent glycosyl-enzyme intermediate
    • GP Connelly SG Withers LP McIntosh 2000 Analysis of the dynamic properties of Bacillus circulans xylanase upon formation of a covalent glycosyl-enzyme intermediate Prot Sci 9 512 524 10.1110/ps.9.3.512 (Pubitemid 30171642)
    • (2000) Protein Science , vol.9 , Issue.3 , pp. 512-524
    • Connelly, G.P.1    Withers, S.G.2    McIntosh, L.P.3
  • 12
    • 0028979982 scopus 로고
    • Abnormally high pKa of an active-site glutamic acid residue in Bacillus circulans xylanase. The role of electrostatic interactions
    • J Davoodi WW Wakarchuk RL Campbell PR Carey WK Surewicz 1995 Abnormally high pKa of an active-site glutamic acid residue in Bacillus circulans xylanase. The role of electrostatic interactions Eur J Biochem 232 839 843
    • (1995) Eur J Biochem , vol.232 , pp. 839-843
    • Davoodi, J.1    Wakarchuk, W.W.2    Campbell, R.L.3    Carey, P.R.4    Surewicz, W.K.5
  • 13
    • 0029400480 scopus 로고
    • NMRpipe-a multidimensional spectral processing system based on UNIX pipes
    • 10.1007/BF00197809
    • F Delaglio S Grzesiek GW Vuister G Zhu J Pfeifer A Bax 1995 NMRpipe-a multidimensional spectral processing system based on UNIX pipes J Biomol NMR 6 277 293 10.1007/BF00197809
    • (1995) J Biomol NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 14
    • 33747593473 scopus 로고    scopus 로고
    • Use of PYMOL as a communications tool for molecular science
    • WL DeLano 2004 Use of PYMOL as a communications tool for molecular science Abstr Pap Am Chem Soc 228 U313 U314
    • (2004) Abstr Pap Am Chem Soc , vol.228
    • Delano, W.L.1
  • 15
    • 0020855355 scopus 로고
    • Hydrogen exchange and structural dynamics of proteins and nucleic acids
    • 10.1017/S0033583500005217
    • SW Englander NR Kallenbach 1983 Hydrogen exchange and structural dynamics of proteins and nucleic acids Q Rev Biophys 16 521 655 10.1017/ S0033583500005217
    • (1983) Q Rev Biophys , vol.16 , pp. 521-655
    • Englander, S.W.1    Kallenbach, N.R.2
  • 16
    • 0028503463 scopus 로고
    • 15N longitudinal decay and chemical exchange rates of systems in slow equilibrium
    • 10.1007/BF00404280
    • 15N longitudinal decay and chemical exchange rates of systems in slow equilibrium J Biomol NMR 4 727 734 10.1007/BF00404280
    • (1994) J Biomol NMR , vol.4 , pp. 727-734
    • Farrow, N.A.1    Zhang, O.2    Forman-Kay, J.D.3    Kay, L.E.4
  • 17
    • 0025288350 scopus 로고
    • Elimination of cross-relaxation effects from two-dimensional chemical-exchange spectra of macromolecules
    • DOI 10.1021/ja00163a014
    • J Fejzo WM Westler S Macura JL Markley 1990 Elimination of cross-relaxation effects from 2-dimensional chemical-exchange spectra of macromolecules J Am Chem Soc 112 2574 2577 10.1021/ja00163a014 (Pubitemid 20186165)
    • (1990) Journal of the American Chemical Society , vol.112 , Issue.7 , pp. 2574-2577
    • Fejzo, J.1    Westler, W.M.2    Macura, S.3    Markley, J.L.4
  • 18
  • 19
    • 58149476769 scopus 로고    scopus 로고
    • A summary of the measured pK values of the ionizable groups in folded proteins
    • GR Grimsley JM Scholtz CN Pace 2009 A summary of the measured pK values of the ionizable groups in folded proteins Prot Sci 18 247 251
    • (2009) Prot Sci , vol.18 , pp. 247-251
    • Grimsley, G.R.1    Scholtz, J.M.2    Pace, C.N.3
  • 20
    • 0024500323 scopus 로고
    • 13C NMR and correlation with kinetic studies
    • DOI 10.1021/bi00431a023
    • 13C NMR and correlation with kinetic studies Biochemistry 28 2116 2124 10.1021/bi00431a023 (Pubitemid 19084439)
    • (1989) Biochemistry , vol.28 , Issue.5 , pp. 2116-2124
    • Grissom, C.B.1    Markley, J.L.2
  • 21
    • 0036001159 scopus 로고    scopus 로고
    • a values of catalytic groups in enzyme active sites
    • DOI 10.1080/15216540211468
    • TK Harris GJ Turner 2002 Structural basis of perturbed pK(a) values of catalytic groups in enzyme active sites IUBMB Life 53 85 98 10.1080/ 15216540211468 (Pubitemid 34553129)
    • (2002) IUBMB Life , vol.53 , Issue.2 , pp. 85-98
    • Harris, T.K.1    Turner, G.J.2
  • 22
    • 9344263447 scopus 로고    scopus 로고
    • Infrequent cavity-forming fluctuations in HPr from Staphylococcus carnosus revealed by pressure- and temperature-dependent tyrosine ring flips
    • DOI 10.1110/ps.04877104
    • M Hattori H Li H Yamada K Akasaka W Hengstenberg W Gronwald HR Kalbitzer 2004 Infrequent cavity-forming fluctuations in HPr from Staphylococcus carnosus revealed by pressure- and temperature-dependent tyrosine ring flips Prot Sci 13 3104 3114 10.1110/ps.04877104 (Pubitemid 39557782)
    • (2004) Protein Science , vol.13 , Issue.12 , pp. 3104-3114
    • Hattori, M.1    Li, H.2    Yamada, H.3    Akasaka, K.4    Hengstenberg, W.5    Gronwald, W.6    Kalbitzer, H.R.7
  • 23
    • 0025365762 scopus 로고
    • 15N NMR spectroscopy: Use of the INEPT experiment to follow individual amides in detergent-solubilized M13 coat protein
    • DOI 10.1021/bi00478a027
    • 15N NMR spectroscopy: use of the INEPT experiment to follow individual amides in detergent-solubilized M13 coat protein Biochemistry 29 6303 6313 10.1021/bi00478a027 (Pubitemid 20222249)
    • (1990) Biochemistry , vol.29 , Issue.26 , pp. 6303-6313
    • Henry, G.D.1    Sykes, B.D.2
  • 24
    • 54049086941 scopus 로고    scopus 로고
    • Identification of new, well-populated amino-acid sidechain rotamers involving hydroxyl-hydrogen atoms and sulfhydryl-hydrogen atoms
    • 10.1186/1472-6807-8-41
    • BK Ho DA Agard 2008 Identification of new, well-populated amino-acid sidechain rotamers involving hydroxyl-hydrogen atoms and sulfhydryl-hydrogen atoms BMC Struct Biol 8 41 10.1186/1472-6807-8-41
    • (2008) BMC Struct Biol , vol.8 , pp. 41
    • Ho, B.K.1    Agard, D.A.2
  • 25
    • 67549086082 scopus 로고    scopus 로고
    • Understanding the functional roles of amino acid residues in enzyme catalysis
    • 10.1016/j.jmb.2009.05.015
    • GL Holliday JBO Mitchell JM Thornton 2009 Understanding the functional roles of amino acid residues in enzyme catalysis J Mol Biol 390 560 577 10.1016/j.jmb.2009.05.015
    • (2009) J Mol Biol , vol.390 , pp. 560-577
    • Holliday, G.L.1    Mitchell, J.B.O.2    Thornton, J.M.3
  • 26
    • 0013994339 scopus 로고
    • Hydrogen exchange in proteins
    • 10.1016/S0065-3233(08)60129-1
    • A Hvidt SO Nielsen 1966 Hydrogen exchange in proteins Adv Prot Chem 21 287 386 10.1016/S0065-3233(08)60129-1
    • (1966) Adv Prot Chem , vol.21 , pp. 287-386
    • Hvidt, A.1    Nielsen, S.O.2
  • 27
    • 0030797606 scopus 로고    scopus 로고
    • Application of phase-modulated CLEAN chemical EXchange spectroscopy (CLEANEX-PM) to detect water - Protein proton exchange and intermolecular NOEs
    • DOI 10.1021/ja970160j
    • TL Hwang S Mori AJ Shaka PCM van Zijl 1997 Application of phase-modulated CLEAN chemical EXchange spectroscopy (CLEANEX-PM) to detect water-protein proton exchange and intermolecular NOEs J Am Chem Soc 119 6203 6204 10.1021/ja970160j (Pubitemid 27314859)
    • (1997) Journal of the American Chemical Society , vol.119 , Issue.26 , pp. 6203-6204
    • Hwang, T.-L.1    Mori, S.2    Shaka, A.J.3    Van Zijl, P.C.M.4
  • 28
    • 0000165109 scopus 로고
    • Isotope-filtered 2D NMR of a protein peptide complex: Study of a skeletal-muscle myosin light chain kinase fragment bound to calmodulin
    • 10.1021/ja00033a019
    • M Ikura A Bax 1992 Isotope-filtered 2D NMR of a protein peptide complex: study of a skeletal-muscle myosin light chain kinase fragment bound to calmodulin J Am Chem Soc 114 2433 2440 10.1021/ja00033a019
    • (1992) J Am Chem Soc , vol.114 , pp. 2433-2440
    • Ikura, M.1    Bax, A.2
  • 30
    • 0031283399 scopus 로고    scopus 로고
    • Complete measurement of the pK(a) values of the carboxyl and imidazole groups in Bacillus circulans xylanase
    • MD Joshi A Hedberg LP McIntosh 1997 Complete measurement of the pKa values of the carboxyl and imidazole groups in Bacillus circulans xylanase Prot Sci 6 2667 2670 10.1002/pro.5560061224 (Pubitemid 28006709)
    • (1997) Protein Science , vol.6 , Issue.12 , pp. 2667-2670
    • Joshi, M.D.1    Hedberg, A.2    McIntosh, L.P.3
  • 31
    • 0035964164 scopus 로고    scopus 로고
    • Dissecting the electrostatic interactions and pH-dependent activity of a family 11 glycosidase
    • DOI 10.1021/bi0105429
    • MD Joshi G Sidhu JE Nielsen GD Brayer SG Withers LP McIntosh 2001 Dissecting the electrostatic interactions and pH-dependent activity of a family 11 glycosidase Biochemistry 40 10115 10139 10.1021/bi0105429 (Pubitemid 32800119)
    • (2001) Biochemistry , vol.40 , Issue.34 , pp. 10115-10139
    • Joshi, M.D.1    Sidhu, G.2    Nielsen, J.E.3    Brayer, G.D.4    Withers, S.G.5    McIntosh, L.P.6
  • 32
    • 33745356391 scopus 로고
    • Contact electron-spin coupling of nuclear magnetic moments
    • 1959JChPh.30.11K 10.1063/1.1729860
    • M Karplus 1959 Contact electron-spin coupling of nuclear magnetic moments J Chem Phys 30 11 15 1959JChPh..30...11K 10.1063/1.1729860
    • (1959) J Chem Phys , vol.30 , pp. 11-15
    • Karplus, M.1
  • 33
    • 0015937171 scopus 로고
    • A nuclear magnetic resonance study of bovine pancreatic trypsin-inhibitor. Tyrosine titrations and backbone NH groups
    • 10.1021/bi00731a012
    • S Karplus GH Snyder BD Sykes 1973 A nuclear magnetic resonance study of bovine pancreatic trypsin-inhibitor. Tyrosine titrations and backbone NH groups Biochemistry 12 1323 1329 10.1021/bi00731a012
    • (1973) Biochemistry , vol.12 , pp. 1323-1329
    • Karplus, S.1    Snyder, G.H.2    Sykes, B.D.3
  • 34
    • 0030610243 scopus 로고    scopus 로고
    • PK(a) measurements from nuclear magnetic resonance for the B1 and B2 immunoglobulin G-binding domains of protein G: Comparison with calculated values for nuclear magnetic resonance and x-ray structures
    • DOI 10.1021/bi9630927
    • D Khare P Alexander J Antosiewicz P Bryan M Gilson J Orban 1997 pK(a) measurements from nuclear magnetic resonance for the B1 and B2 immunoglobulin G-binding domains of protein G: Comparison with calculated values for nuclear magnetic resonance and x-ray structures Biochemistry 36 3580 3589 10.1021/bi9630927 (Pubitemid 27143512)
    • (1997) Biochemistry , vol.36 , Issue.12 , pp. 3580-3589
    • Khare, D.1    Alexander, P.2    Antosiewicz, J.3    Bryan, P.4    Gilson, M.5    Orban, J.6
  • 35
    • 0025093242 scopus 로고
    • +-ATPase of Escherichia coli and NMR studies
    • DOI 10.1016/0014-5793(90)80442-L
    • HW Kim JA Perez SJ Ferguson ID Campbell 1990 The specific incorporation of labelled aromatic amino acids into proteins through growth of bacteria in the presence of glyphosate. Application to fluorotryptophan labelling to the H(+)-ATPase of Escherichia coli and NMR studies FEBS Lett 272 34 36 10.1016/0014-5793(90)80442-L (Pubitemid 20348975)
    • (1990) FEBS Letters , vol.272 , Issue.1-2 , pp. 34-36
    • Kim, H.-W.1    Perez, J.A.2    Ferguson, S.J.3    Campbell, I.D.4
  • 36
    • 0025338948 scopus 로고
    • Hydroxyl hydrogen conformations in trypsin determined by the neutron diffraction solvent difference map method: Relative importance of steric and electrostatic factors in defining hydrogen-bonding geometries
    • DOI 10.1073/pnas.87.12.4468
    • AA Kossiakoff J Shpungin MD Sintchak 1990 Hydroxyl hydrogen conformations in trypsin determined by the neutron-diffraction solvent difference map method: relative importance of steric and electrostatic factors in defining hydrogen-bonding geometries Proc Natl Acad Sci 87 4468 4472 1990PNAS...87.4468K 10.1073/pnas.87.12.4468 (Pubitemid 20204122)
    • (1990) Proceedings of the National Academy of Sciences of the United States of America , vol.87 , Issue.12 , pp. 4468-4472
    • Kossiakoff, A.A.1    Shpungin, J.2    Sintchak, M.D.3
  • 38
    • 0027530942 scopus 로고
    • 5-3- ketosteroid isomerase
    • YK Li A Kuliopulos AS Mildvan P Talalay 1993 Environments and mechanistic roles of the tyrosine residues of delta-5-3-ketosteroid isomerase Biochemistry 32 1816 1824 10.1021/bi00058a016 (Pubitemid 23066456)
    • (1993) Biochemistry , vol.32 , Issue.7 , pp. 1816-1824
    • Li, Y.-K.1    Kuliopulos, A.2    Mildvan, A.S.3    Talalay, P.4
  • 39
    • 0030051552 scopus 로고    scopus 로고
    • Proton exchange rates from amino acid side chains - Implications for image contrast
    • DOI 10.1002/mrm.1910350106
    • E Liepinsh G Otting 1996 Proton exchange rates from amino acid side chains-implications for image contrast Magn Reson Med 35 30 42 10.1002/mrm.1910350106 (Pubitemid 26017917)
    • (1996) Magnetic Resonance in Medicine , vol.35 , Issue.1 , pp. 30-42
    • Liepinsh, E.1    Otting, G.2
  • 40
    • 0026925802 scopus 로고
    • NMR spectroscopy of hydroxyl protons in aqueous solutions of peptides and proteins
    • 10.1007/BF02192808
    • E Liepinsh G Otting K Wüthrich 1992 NMR spectroscopy of hydroxyl protons in aqueous solutions of peptides and proteins J Biomol NMR 2 447 465 10.1007/BF02192808
    • (1992) J Biomol NMR , vol.2 , pp. 447-465
    • Liepinsh, E.1    Otting, G.2    Wüthrich, K.3
  • 41
    • 0030832007 scopus 로고    scopus 로고
    • Mechanistic roles of tyrosine 149 and serine 124 in UDP-galactose 4- epimerase from Escherichia coli
    • DOI 10.1021/bi970430a
    • YJ Liu JB Thoden J Kim E Berger AM Gulick FJ Ruzicka HM Holden PA Frey 1997 Mechanistic roles of tyrosine 149 and serine 124 in UDP-galactose 4-epimerase from Escherichia coli Biochemistry 36 10675 10684 10.1021/bi970430a (Pubitemid 27382557)
    • (1997) Biochemistry , vol.36 , Issue.35 , pp. 10675-10684
    • Liu, Y.1    Thoden, J.B.2    Kim, J.3    Berger, E.4    Gulick, A.M.5    Ruzicka, F.J.6    Holden, H.M.7    Frey, P.A.8
  • 42
    • 27244451944 scopus 로고    scopus 로고
    • Triple-resonance methods for complete resonance assignment of aromatic protons and directly bound heteronuclei in histidine and tryptophan residues
    • DOI 10.1007/s10858-005-1195-4
    • F Löhr VV Rogov M Shi F Bernhard V Dötsch 2005 Triple-resonance methods for complete resonance assignment of aromatic protons and directly bound heteronuclei in histidine and tryptophan residues J Biomol NMR 32 4 309 328 10.1007/s10858-005-1195-4 (Pubitemid 41511512)
    • (2005) Journal of Biomolecular NMR , vol.32 , Issue.4 , pp. 309-328
    • Lohr, F.1    Rogov, V.V.2    Shi, M.3    Bernhard, F.4    Dotsch, V.5
  • 43
    • 33947608952 scopus 로고    scopus 로고
    • Improved pulse sequences for sequence specific assignment of aromatic proton resonances in proteins
    • DOI 10.1007/s10858-006-9128-4
    • F Löhr R Hansel VV Rogov V Dötsch 2007 Improved pulse sequences for sequence specific assignment of aromatic proton resonances in proteins J Biomol NMR 37 3 205 224 10.1007/s10858-006-9128-4 (Pubitemid 46476998)
    • (2007) Journal of Biomolecular NMR , vol.37 , Issue.3 , pp. 205-224
    • Lohr, F.1    Hansel, R.2    Rogov, V.V.3    Dotsch, V.4
  • 44
    • 1442323777 scopus 로고    scopus 로고
    • High-resolution crystal structure of Arthrobacter aurescens chondroitin AC lyase: An enzyme-substrate complex defines the catalytic mechanism
    • DOI 10.1016/j.jmb.2003.12.071, PII S0022283604000269
    • VV Lunin YG Li RJ Linhardt H Miyazono M Kyogashima T Kaneko AW Bell M Cygler 2004 High resolution crystal structure of Arthrobacter aurescens chondroitin AC lyase: an enzyme-substrate complex defines the catalytic mechanism J Mol Biol 337 367 386 10.1016/j.jmb.2003.12.071 (Pubitemid 38293405)
    • (2004) Journal of Molecular Biology , vol.337 , Issue.2 , pp. 367-386
    • Lunin, V.V.1    Li, Y.2    Linhardt, R.J.3    Miyazono, H.4    Kyogashima, M.5    Kaneko, T.6    Bell, A.W.7    Cygler, M.8
  • 46
    • 80755187569 scopus 로고    scopus 로고
    • Dissecting electrostatic interactions in Bacillus circulans xylanase through NMR-monitored pH titrations
    • (in press)
    • McIntosh LP, Naito D, Baturin SJ, Okon M, Joshi MD, Nielsen JE (2011) Dissecting electrostatic interactions in Bacillus circulans xylanase through NMR-monitored pH titrations. J Biomol NMR (in press)
    • (2011) J Biomol NMR
    • McIntosh, L.P.1    Naito, D.2    Baturin, S.J.3    Okon, M.4    Joshi, M.D.5    Nielsen, J.E.6
  • 47
    • 0028244925 scopus 로고
    • Identification of glutamic acid 78 as the active site nucleophile in Bacillus subtilis xylanase using electrospray tandem mass spectrometry
    • DOI 10.1021/bi00189a002
    • SC Miao L Ziser R Aebersold SG Withers 1994 Identification of glutamic acid 78 as the active site nucleophile in Bacillus subtilis xylanase using electrospray tandem mass-spectrometry Biochemistry 33 7027 7032 10.1021/bi00189a002 (Pubitemid 24208736)
    • (1994) Biochemistry , vol.33 , Issue.23 , pp. 7027-7032
    • Miao, S.1    Ziser, L.2    Aebersold, R.3    Withers, S.G.4
  • 48
    • 0025004276 scopus 로고
    • Rates and energetics of tyrosine ring flips in yeast iso-2-cytochrome c
    • DOI 10.1021/bi00485a006
    • BT Nall EH Zuniga 1990 Rates and energetics of tyrosine ring flips in yeast iso-2-cytochrome c Biochemistry 29 7576 7584 10.1021/bi00485a006 (Pubitemid 20279173)
    • (1990) Biochemistry , vol.29 , Issue.33 , pp. 7576-7584
    • Nall, B.T.1    Zuniga, E.H.2
  • 49
    • 37049140963 scopus 로고
    • Carbon 13 nuclear magnetic resonance study of tyrosine titrations
    • Norton RS, Bradbury JH (1974) Carbon 13 nuclear magnetic resonance study of tyrosine titrations. J Chem Soc Chem Comm 870-871
    • (1974) J Chem Soc Chem Comm , pp. 870-871
    • Norton, R.S.1    Bradbury, J.H.2
  • 50
    • 0016825166 scopus 로고
    • Studies of individual carbon sites of proteins in solution by natural abundance carbon 13 nuclear magnetic resonance spectroscopy - Relaxation behavior
    • E Oldfield RS Norton A Allerhand 1975 Studies of individual carbon sites of proteins in solution by natural abundance carbon 13 nuclear magnetic resonance spectroscopy - relaxation behavior J Biol Chem 250 6368 6380
    • (1975) J Biol Chem , vol.250 , pp. 6368-6380
    • Oldfield, E.1    Norton, R.S.2    Allerhand, A.3
  • 51
    • 0016840028 scopus 로고
    • Studies of individual carbon sites of proteins in solution by natural abundance carbon 13 nuclear magnetic resonance spectroscopy-strategies for assignments
    • E Oldfield RS Norton A Allerhand 1975 Studies of individual carbon sites of proteins in solution by natural abundance carbon 13 nuclear magnetic resonance spectroscopy-strategies for assignments J Biol Chem 250 6381 6402
    • (1975) J Biol Chem , vol.250 , pp. 6381-6402
    • Oldfield, E.1    Norton, R.S.2    Allerhand, A.3
  • 53
    • 0027456412 scopus 로고
    • Tautomeric states of the active-site histidines of phosphorylated and unphosphorylated III(Glc), a signal-transducing protein from Escherichia coli, using two-dimensional heteronuclear NMR techniques
    • JG Pelton DA Torchia ND Meadow S Roseman 1993 Tautomeric states of the active-site histidines of phosphorylated and unphosphorylated Iii(Glc), a signal-transducing protein from Escherichia coli, using 2-dimensional heteronuclear NMR techniques Prot Sci 2 543 558 10.1002/pro.5560020406 (Pubitemid 23119305)
    • (1993) Protein Science , vol.2 , Issue.4 , pp. 543-558
    • Pelton, J.G.1    Torchia, D.A.2    Meadow, N.D.3    Roseman, S.4
  • 54
    • 0029843569 scopus 로고    scopus 로고
    • Characterization of a buried neutral histidine residue in Bacillus circulans xylanase: NMR assignments, pH titration, and hydrogen exchange
    • LA Plesniak GP Connelly WW Wakarchuk LP McIntosh 1996 Characterization of a buried neutral histidine residue in Bacillus circulans xylanase: NMR assignments, pH titration, and hydrogen exchange Prot Sci 5 2319 2328 10.1002/pro.5560051118 (Pubitemid 26384470)
    • (1996) Protein Science , vol.5 , Issue.11 , pp. 2319-2328
    • Plesniak, L.A.1    Connelly, G.P.2    Wakarchuk, W.W.3    Mcintosh, L.P.4
  • 55
    • 0029955152 scopus 로고    scopus 로고
    • Secondary structure and NMR assignments of Bacillus circulans xylanase
    • LA Plesniak WW Wakarchuk LP McIntosh 1996 Secondary structure and NMR assignments of Bacillus circulans xylanase Prot Sci 5 1118 1135 10.1002/pro.5560050614 (Pubitemid 26172900)
    • (1996) Protein Science , vol.5 , Issue.6 , pp. 1118-1135
    • Plesniak, L.A.1    Wakarchuk, W.W.2    Mcintosh, L.P.3
  • 57
    • 35448960711 scopus 로고    scopus 로고
    • Complexity of aromatic ring-flip motions in proteins: Y97 ring dynamics in cytochrome c observed by cross-relaxation suppressed exchange NMR spectroscopy
    • DOI 10.1007/s10858-007-9186-2
    • DK Rao AK Bhuyan 2007 Complexity of aromatic ring-flip motions in proteins: Y97 ring dynamics in cytochrome c observed by cross-relaxation suppressed exchange NMR spectroscopy J Biomol NMR 39 3 187 196 10.1007/s10858-007-9186-2 (Pubitemid 47617503)
    • (2007) Journal of Biomolecular NMR , vol.39 , Issue.3 , pp. 187-196
    • Krishna Rao, D.1    Bhuyan, A.K.2
  • 58
    • 0018118592 scopus 로고
    • Carbon-13 NMR chemical shifts of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH
    • R Richarz K Wüthrich 1978 Carbon-13 NMR chemical shifts of the common amino acid residues measured in aqueous solutions of linear tetrapeptides H-Gly-Gly-X-L-Ala-OH Biopolymers 17 2133 2141 10.1002/bip.1978.360170908 (Pubitemid 9015225)
    • (1978) Biopolymers , vol.17 , Issue.9 , pp. 2133-2141
    • Richarz, R.1    Wuthrich, K.2
  • 59
    • 0347722841 scopus 로고    scopus 로고
    • Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients
    • PII S0079656598000259
    • M Sattler J Schleucher C Griesinger 1999 Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients Prog Nucl Magn Reson Spect 34 93 158 10.1016/S0079-6565(98)00025-9 (Pubitemid 129595216)
    • (1999) Progress in Nuclear Magnetic Resonance Spectroscopy , vol.34 , Issue.2 , pp. 93-158
    • Sattler, M.1    Schleucher, J.2    Griesinger, C.3
  • 60
    • 0033609135 scopus 로고    scopus 로고
    • Sugar ring distortion in the glycosyl-enzyme intermediate of a family G/11 xylanase
    • DOI 10.1021/bi982946f
    • G Sidhu SG Withers NT Nguyen LP McIntosh L Ziser GD Brayer 1999 Sugar ring distortion in the glycosyl-enzyme intermediate of a family G/11 xylanase Biochemistry 38 5346 5354 10.1021/bi982946f (Pubitemid 29211219)
    • (1999) Biochemistry , vol.38 , Issue.17 , pp. 5346-5354
    • Sidhu, G.1    Withers, S.G.2    Nguyen, N.T.3    McIntosh, L.P.4    Ziser, L.5    Brayer, G.D.6
  • 61
    • 0035941549 scopus 로고    scopus 로고
    • Aromatic ring-flipping in supercooled water: Implications for NMR-based structural biology of proteins
    • DOI 10.1021/ja003220l
    • JJ Skalicky JL Mills S Sharma T Szyperski 2001 Aromatic ring flipping in supercooled water: implications for NMR-based structural biology of proteins J Am Chem Soc 123 388 397 10.1021/ja003220l (Pubitemid 32105128)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.3 , pp. 388-397
    • Skalicky, J.J.1    Mills, J.L.2    Sharma, S.3    Szyperski, T.4
  • 62
    • 0016819380 scopus 로고
    • 1H nuclear magnetic resonance spectrum of bovine pancreatic trypsin inhibitor
    • 10.1021/bi00688a008
    • 1H nuclear magnetic resonance spectrum of bovine pancreatic trypsin inhibitor Biochemistry 14 3765 3777 10.1021/bi00688a008
    • (1975) Biochemistry , vol.14 , pp. 3765-3777
    • Snyder, G.H.1    Rowan, R.2    Karplus, S.3    Sykes, B.D.4
  • 63
    • 0033616634 scopus 로고    scopus 로고
    • Evidence for a two-base mechanism involving tyrosine-265 from arginine- 219 mutants of alanine racemase
    • DOI 10.1021/bi982924t
    • SX Sun MD Toney 1999 Evidence for a two-base mechanism involving tyrosine-265 from arginine-219 mutants of alanine racemase Biochemistry 38 4058 4065 10.1021/bi982924t (Pubitemid 29160061)
    • (1999) Biochemistry , vol.38 , Issue.13 , pp. 4058-4065
    • Sun, S.1    Toney, M.D.2
  • 64
    • 4344645436 scopus 로고    scopus 로고
    • a value of iron-binding ligand Tyr188 and its implication in iron release and anion binding of human transferrin
    • DOI 10.1016/j.febslet.2004.07.076, PII S0014579304009561
    • a value of iron-binding ligand Tyr188 and its implication in iron release and anion binding of human transferrin FEBS Lett 573 181 185 10.1016/j.febslet.2004.07.076 (Pubitemid 39141055)
    • (2004) FEBS Letters , vol.573 , Issue.1-3 , pp. 181-185
    • Sun, X.1    Sun, H.2    Ge, R.3    Richter, M.4    Woodworth, R.C.5    Mason, A.B.6    He, Q.-Y.7
  • 66
    • 33646145955 scopus 로고    scopus 로고
    • PK values of the ionizable groups of proteins
    • 10.1110/ps.051840806
    • RL Thurlkill GR Grimsley JM Scholtz CN Pace 2006 pK values of the ionizable groups of proteins Prot Sci 15 1214 1218 10.1110/ps.051840806
    • (2006) Prot Sci , vol.15 , pp. 1214-1218
    • Thurlkill, R.L.1    Grimsley, G.R.2    Scholtz, J.M.3    Pace, C.N.4
  • 68
    • 0019318643 scopus 로고
    • 1H-NMR at variable pressure
    • 10.1016/0014-5793(80)80198-0
    • 1H-NMR at variable pressure FEBS Lett 112 280 284 10.1016/0014-5793(80)80198-0
    • (1980) FEBS Lett , vol.112 , pp. 280-284
    • Wagner, G.1
  • 69
    • 0006356190 scopus 로고
    • Proton NMR-Studies of aromatic residues in basic pancreatic trypsin inhibitor (BPTI)
    • G Wagner K Wüthrich 1975 Proton NMR-Studies of aromatic residues in basic pancreatic trypsin inhibitor (BPTI) J Magn Reson 20 435 445
    • (1975) J Magn Reson , vol.20 , pp. 435-445
    • Wagner, G.1    Wüthrich, K.2
  • 70
    • 0018137537 scopus 로고
    • Dynamic model of globular protein conformations based on NMR studies in solution
    • DOI 10.1038/275247a0
    • G Wagner K Wüthrich 1978 Dynamic model of globular protein conformations based on NMR studies in solution Nature 275 247 248 1978Natur.275..247W 10.1038/275247a0 (Pubitemid 9008047)
    • (1978) Nature , vol.275 , Issue.5677 , pp. 247-248
    • Wagner, G.1    Wuethrich, K.2
  • 72
    • 0028211360 scopus 로고
    • Mutational and crystallographic analyses of the active site residues of the Bacillus circulans xylanase
    • WW Wakarchuk RL Campbell WL Sung J Davoodi M Yaguchi 1994 Mutational and crystallographic analyses of the active site residues of the Bacillus circulans xylanase Prot Sci 3 467 475 10.1002/pro.5560030312 (Pubitemid 24103718)
    • (1994) Protein Science , vol.3 , Issue.3 , pp. 467-475
    • Wakarchuk, W.W.1    Campbell, R.L.2    Sung, W.L.3    Davoodi, J.4    Yaguchi, M.5
  • 76
    • 0033614004 scopus 로고    scopus 로고
    • Asparagine and glutamine: Using hydrogen atom contacts in the choice of side-chain amide orientation
    • DOI 10.1006/jmbi.1998.2401
    • JM Word SC Lovell JS Richardson DC Richardson 1999 Asparagine and glutamine: using hydrogen atom contacts in the choice of side chain amide orientation J Mol Biol 285 1735 1747 10.1006/jmbi.1998.2401 (Pubitemid 29060467)
    • (1999) Journal of Molecular Biology , vol.285 , Issue.4 , pp. 1735-1747
    • Word, J.M.1    Lovell, S.C.2    Richardson, J.S.3    Richardson, D.C.4
  • 77
    • 0016433835 scopus 로고
    • NMR investigations of dynamics of aromatic amino acid residues in basic pancreatic trypsin inhibitor
    • 10.1016/0014-5793(75)80504-7
    • K Wüthrich G Wagner 1975 NMR investigations of dynamics of aromatic amino acid residues in basic pancreatic trypsin inhibitor FEBS Lett 50 265 268 10.1016/0014-5793(75)80504-7
    • (1975) FEBS Lett , vol.50 , pp. 265-268
    • Wüthrich, K.1    Wagner, G.2
  • 78
  • 79
    • 0027310404 scopus 로고
    • Complete assignments of magnetic resonances of ribonuclease H from Escherichia coli by double- and triple-resonance 2D and 3D NMR spectroscopies
    • T Yamazaki M Yoshida K Nagayama 1993 Complete assignments of magnetic resonances of ribonuclease H from Escherichia coli by double-resonance and triple-resonance 2D and 3D NMR spectroscopies Biochemistry 32 5656 5669 10.1021/bi00072a023 (Pubitemid 23178533)
    • (1993) Biochemistry , vol.32 , Issue.21 , pp. 5656-5669
    • Yamazaki, T.1    Yoshida, M.2    Nagayama, K.3
  • 81
    • 78549235443 scopus 로고    scopus 로고
    • Topoisomerases and site-specific recombinases: Similarities in structure and mechanism
    • 10.3109/10409238.2010.513375
    • W Yang 2010 Topoisomerases and site-specific recombinases: similarities in structure and mechanism Crit Rev Biochem Mol Biol 45 520 534 10.3109/10409238.2010.513375
    • (2010) Crit Rev Biochem Mol Biol , vol.45 , pp. 520-534
    • Yang, W.1
  • 82
    • 0030808350 scopus 로고    scopus 로고
    • Methods for measurement of intermolecular NOEs by multinuclear NMR spectroscopy: Application to a bacteriophage λ N-peptide/boxB RNA complex
    • DOI 10.1021/ja970224q
    • C Zwahlen P Legault SJF Vincent J Greenblatt R Konrat LE Kay 1997 Methods for measurement of intermolecular NOEs by multinuclear NMR spectroscopy: application to a bacteriophage λ N-peptide/boxB RNA complex J Am Chem Soc 119 6711 6721 10.1021/ja970224q (Pubitemid 27343493)
    • (1997) Journal of the American Chemical Society , vol.119 , Issue.29 , pp. 6711-6721
    • Zwahlen, C.1    Legault, P.2    Vincent, S.J.F.3    Greenblatt, J.4    Konrat, R.5    Kay, L.E.6


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