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Volumn 60, Issue 2-3, 2014, Pages 109-129

PH-dependent random coil 1H, 13C, and 15N chemical shifts of the ionizable amino acids: A guide for protein pK a measurements

Author keywords

Chemical shift; Deuterium isotope shift; Hydrogen exchange; pH titration; Protein electrostatics; Scalar coupling

Indexed keywords

AMINO ACID; ARGININE; ASPARTIC ACID; CARBON 13; CARBOXYLIC ACID; CYSTEINE; DEUTERIUM; GLUTAMIC ACID; HISTAMINE; LYSINE; NITROGEN 15; PHOSPHOAMINO ACID; POLYPEPTIDE; TRIPEPTIDE; TYROSINE; CARBON; HYDROGEN; NITROGEN; PROTEIN;

EID: 84922003154     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-014-9862-y     Document Type: Article
Times cited : (163)

References (227)
  • 1
    • 33847085401 scopus 로고
    • 15N NMR shifts and coupling-constants in aqueous imidazole and 1-methylimidazole - Comments on estimation of tautomeric equilibrium-constants for aqueous histidine
    • 15N NMR shifts and coupling-constants in aqueous imidazole and 1-methylimidazole - comments on estimation of tautomeric equilibrium-constants for aqueous histidine. J Am Chem Soc 102:2881-2887
    • (1980) J Am Chem Soc , vol.102 , pp. 2881-2887
    • Alei, M.1    Morgan, L.O.2    Wageman, W.E.3    Whaley, T.W.4
  • 2
    • 81055157643 scopus 로고    scopus 로고
    • Progress in the prediction of pKa values in proteins
    • Alexov E et al (2011) Progress in the prediction of pKa values in proteins. Proteins 79:3260-3275
    • (2011) Proteins , vol.79 , pp. 3260-3275
    • Alexov, E.1
  • 3
    • 84922005857 scopus 로고    scopus 로고
    • Protein apparent dielectric constant and its termperature dependence from remote chemical shift effects
    • 9 Sept 2014 [Epub ahead of print]
    • An L, Wang Y, Zhang N, Yan S, Bax A, Yai L (2014) Protein apparent dielectric constant and its termperature dependence from remote chemical shift effects. J Am Chem Soc 136, 9 Sept 2014 [Epub ahead of print]
    • (2014) J Am Chem Soc 136
    • An, L.1    Wang, Y.2    Zhang, N.3    Yan, S.4    Bax, A.5    Yai, L.6
  • 4
    • 84922005856 scopus 로고
    • The folding, stability and dynamics of T4 lysozyme: A perspective using nuclear magnetic resonance
    • MacMillan Press, London
    • Anderson DE, Lu J, McIntosh LP, Dahlquist FW (1993) The folding, stability and dynamics of T4 lysozyme: a perspective using nuclear magnetic resonance. In: Clore GM, Gronenborn AM (eds) NMR of Proteins, MacMillan Press, London, pp 258-304
    • (1993) Clore GM, Gronenborn AM (Eds) NMR of Proteins , pp. 258-304
    • De, A.1    Lu, J.2    McIntosh, L.P.3    Dahlquist, F.W.4
  • 6
    • 37549044716 scopus 로고    scopus 로고
    • 13C NMR spectroscopy: Application to apo calmodulin
    • 13C NMR spectroscopy: application to apo calmodulin. J Am Chem Soc 129:15805-15813
    • (2007) J Am Chem Soc , vol.129 , pp. 15805-15813
    • Andre, I.1    Linse, S.2    Mulder, F.A.A.3
  • 8
    • 0022925238 scopus 로고
    • 15N NMR spectroscopy of hydrogen-honding interactions in the active-site of serine protease - Evidence for a moving histidine mechanism
    • 15N NMR spectroscopy of hydrogen-honding interactions in the active-site of serine protease - evidence for a moving histidine mechanism. Biochemistry 25:7751-7759
    • (1986) Biochemistry , vol.25 , pp. 7751-7759
    • Bachovchin, W.W.1
  • 9
    • 0000037162 scopus 로고    scopus 로고
    • Contributions of NMR spectroscopy to the study of hydrogen bonds in serine protease active sites
    • Bachovchin WW (2001) Contributions of NMR spectroscopy to the study of hydrogen bonds in serine protease active sites. Magn Reson Chem 39:S199-S213
    • (2001) Magn Reson Chem , vol.39 , pp. 199-S213
    • Bachovchin, W.W.1
  • 10
    • 33947094423 scopus 로고
    • 15N nuclear magnetic-resonance spectroscopy - State of histidine in catalytic triad of alpha-lytic protease - Implications for charge-relay mechanism of peptide-bond cleavage by serine proteases
    • 15N nuclear magnetic-resonance spectroscopy - state of histidine in catalytic triad of alpha-lytic protease - implications for charge-relay mechanism of peptide-bond cleavage by serine proteases. J Am Chem Soc 100:8041-8047
    • (1978) J Am Chem Soc , vol.100 , pp. 8041-8047
    • Bachovchin, W.W.1    Roberts, J.D.2
  • 13
    • 84865182658 scopus 로고    scopus 로고
    • 13C chemical shift signature provides the coordination mode of histidines in zinc-binding proteins
    • 13C chemical shift signature provides the coordination mode of histidines in zinc-binding proteins. J Biomol NMR 53:93-101
    • (2012) J Biomol NMR , vol.53 , pp. 93-101
    • Barraud, P.1    Scubert, M.2    Allain, F.H.T.3
  • 14
    • 0002483857 scopus 로고
    • 13C NMR protonation shifts of amines, carboxylic-acids and amino acids
    • 1975JMagR.20.19B
    • 13C NMR protonation shifts of amines, carboxylic-acids and amino acids. J Magn Reson 20:19-38
    • (1975) J Magn Reson , vol.20 , pp. 19-38
    • Batchelor, J.G.1    Feeney, J.2    Roberts, G.C.K.3
  • 15
    • 80755140499 scopus 로고    scopus 로고
    • Structure, dynamics, and ionization equilibria of the tyrosine residues in Bacillus circulans xylanase
    • Baturin SJ, Okon M, McIntosh LP (2011) Structure, dynamics, and ionization equilibria of the tyrosine residues in Bacillus circulans xylanase. J Biomol NMR 51:379-394
    • (2011) J Biomol NMR , vol.51 , pp. 379-394
    • Baturin, S.J.1    Okon, M.2    McIntosh, L.P.3
  • 16
    • 2442442434 scopus 로고    scopus 로고
    • Long-range nature of the interactions between titratable groups in Bacillus agaradhaerens family 11 xylanase: PH titration of B-agaradhaerens xylanase
    • Betz M, Löhr F, Wienk H, Rüterjans H (2004) Long-range nature of the interactions between titratable groups in Bacillus agaradhaerens family 11 xylanase: pH titration of B-agaradhaerens xylanase. Biochemistry 43:5820-5831
    • (2004) Biochemistry , vol.43 , pp. 5820-5831
    • Betz, M.1    Löhr, F.2    Wienk, H.3    Rüterjans, H.4
  • 17
    • 0033377656 scopus 로고    scopus 로고
    • Random-coil chemical shifts of phosphorylated amino acids
    • Bienkiewicz EA, Lumb KJ (1999) Random-coil chemical shifts of phosphorylated amino acids. J Biomol NMR 15:203-206
    • (1999) J Biomol NMR , vol.15 , pp. 203-206
    • Bienkiewicz, E.A.1    Lumb, K.J.2
  • 19
    • 0039247247 scopus 로고
    • Nitrogen-15 NMR in biological systems
    • Blomberg F, Rüterjans H (1983) Nitrogen-15 NMR in biological systems. Biol Magn Reson 21-73
    • (1983) Biol Magn Reson , pp. 21-73
    • Blomberg F, R.1
  • 22
    • 0032392937 scopus 로고    scopus 로고
    • NJ(13C, O1H) coupling constants of intramolecularly hydrogen-bonded compounds
    • Borisov EV, Zhang W, Bolvig S, Hansen PE (1998) nJ(13C, O1H) coupling constants of intramolecularly hydrogen-bonded compounds. Magn Reson Chem 36:S104-S110
    • (1998) Magn Reson Chem , vol.36 , pp. 104-S110
    • Borisov, E.V.1    Zhang, W.2    Bolvig, S.3    Hansen, P.E.4
  • 25
    • 84895192404 scopus 로고    scopus 로고
    • Detection and characterization of serine and threonine hydroxyl protons in Bacillus circulans xylanase by NMR spectroscopy
    • Brockerman JA, Okon M, McIntosh LP (2014) Detection and characterization of serine and threonine hydroxyl protons in Bacillus circulans xylanase by NMR spectroscopy. J Biomol NMR 58:17-25
    • (2014) J Biomol NMR , vol.58 , pp. 17-25
    • Brockerman, J.A.1    Okon, M.2    McIntosh, L.P.3
  • 27
    • 0000103150 scopus 로고
    • Chemical shifts in the nuclear magnetic resonance spectra of molecules containing polar groups
    • Buckingham AD (1960) Chemical shifts in the nuclear magnetic resonance spectra of molecules containing polar groups. Can J Chem 38:300-307
    • (1960) Can J Chem , vol.38 , pp. 300-307
    • Buckingham, A.D.1
  • 28
    • 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
    • 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
    • (1979) Biopolymers , vol.18 , pp. 285-297
    • Bundi, A.1    Wüthrich, K.2
  • 29
    • 84985653913 scopus 로고
    • 1H-NMR titration shifts for studies of polypeptide conformation
    • 1H-NMR titration shifts for studies of polypeptide conformation. Biopolymers 18:299-311
    • (1979) Biopolymers , vol.18 , pp. 299-311
    • Bundi, A.1    Wüthrich, K.2
  • 30
    • 49349130990 scopus 로고
    • Spin-spin coupling and the conformational states of peptide systems
    • Bystrov VF (1976) Spin-spin coupling and the conformational states of peptide systems. Prog Nuc Mag Reson Spect 10:41-81
    • (1976) Prog Nuc Mag Reson Spect , vol.10 , pp. 41-81
    • Bystrov, V.F.1
  • 32
    • 77951667170 scopus 로고    scopus 로고
    • 15N H/D-SOLEXSY experiment for accurate measurement of amide solvent exchange rates: Application to denatured drkN SH3
    • 15N H/D-SOLEXSY experiment for accurate measurement of amide solvent exchange rates: application to denatured drkN SH3. J Biomol NMR 46:227-244
    • (2010) J Biomol NMR , vol.46 , pp. 227-244
    • Chevelkov, V.1    Xue, Y.2    Rao, D.K.3    Forman-Kay, J.D.4    Skrynnikov, N.R.5
  • 34
    • 34548423250 scopus 로고    scopus 로고
    • Carboxyl pKa values, ion pairs, hydrogen bonding, and the pH-dependence of folding the hyperthermophile proteins Sac7d and Sso7d
    • Clark AT, Smith K, Muhandiram R, Edmondson SP, Shriver JW (2007) Carboxyl pKa values, ion pairs, hydrogen bonding, and the pH-dependence of folding the hyperthermophile proteins Sac7d and Sso7d. J Mol Biol 372:992-1008
    • (2007) J Mol Biol , vol.372 , pp. 992-1008
    • Clark, A.T.1    Smith, K.2    Muhandiram, R.3    Edmondson, S.P.4    Shriver, J.W.5
  • 35
    • 0042289481 scopus 로고
    • Observations of amino acid side chains in proteins by NMR methods
    • J.S. Cohen (eds) 2 Wiley Interscience New York
    • Cohen JS, Hughes L, Wooten JB (1983) Observations of amino acid side chains in proteins by NMR methods. In: Cohen JS (ed) Magnetic resonance in biology, vol 2. Wiley Interscience, New York, pp 130-147
    • (1983) Magnetic Resonance in Biology , pp. 130-147
    • Cohen, J.S.1    Hughes, L.2    Wooten, J.B.3
  • 36
    • 0032539528 scopus 로고    scopus 로고
    • Characterization of a buried neutral histidine in Bacillus circulans xylanase: Internal dynamics and interaction with a bound water molecule
    • Connelly GP, McIntosh LP (1998) Characterization of a buried neutral histidine in Bacillus circulans xylanase: internal dynamics and interaction with a bound water molecule. Biochemistry 37:1810-1818
    • (1998) Biochemistry , vol.37 , pp. 1810-1818
    • Connelly, G.P.1    McIntosh, L.P.2
  • 38
    • 0026345864 scopus 로고
    • Structural and thermodynamic consequences of burying a charged residue within the hydrophobic core of T4 lysozyme
    • Daopin S, Anderson DE, Baase WA, Dahlquist FW, Matthews BW (1991) Structural and thermodynamic consequences of burying a charged residue within the hydrophobic core of T4 lysozyme. Biochemistry 30:11521-11529
    • (1991) Biochemistry , vol.30 , pp. 11521-11529
    • Daopin, S.1    Anderson, D.E.2    Baase, W.A.3    Dahlquist, F.W.4    Matthews, B.W.5
  • 39
    • 0037379161 scopus 로고    scopus 로고
    • Tautomerism, acid-base equilibria, and H-bonding of the six histidines in subtilisin BPN' by NMR
    • Day RM et al (2003) Tautomerism, acid-base equilibria, and H-bonding of the six histidines in subtilisin BPN' by NMR. Protein Sci 12:794-810
    • (2003) Protein Sci , vol.12 , pp. 794-810
    • Day, R.M.1
  • 40
    • 70450194574 scopus 로고    scopus 로고
    • Accurate random coil chemical shifts from an analysis of loop regions in native states of proteins
    • De Simone A, Cavalli A, Hsu STD, Vranken W, Vendruscolo M (2009) Accurate random coil chemical shifts from an analysis of loop regions in native states of proteins. J Am Chem Soc 131:16332-16333
    • (2009) J Am Chem Soc , vol.131 , pp. 16332-16333
    • De Simone, A.1    Cavalli, A.2    Hsu, S.T.D.3    Vranken, W.4    Vendruscolo, M.5
  • 41
    • 0000132887 scopus 로고
    • PH-dependence of internal references
    • 1977JMagR.26.527D
    • Demarco A (1977) pH-dependence of internal references. J Magn Reson 26:527-528
    • (1977) J Magn Reson , vol.26 , pp. 527-528
    • Demarco, A.1
  • 42
    • 0035002930 scopus 로고    scopus 로고
    • Application of the deuterium isotope effect on NMR chemical shift to study proton transfer equilibrium
    • Dziembowska T, Rozwadowski Z (2001) Application of the deuterium isotope effect on NMR chemical shift to study proton transfer equilibrium. Curr Org Chem 5:289-313
    • (2001) Curr Org Chem , vol.5 , pp. 289-313
    • Dziembowska, T.1    Rozwadowski, Z.2
  • 43
    • 0021770933 scopus 로고
    • 1H nuclear magnetic-resonance (COSY) - Manifestation of conformational equilibria involving carboxylate groups
    • 1H nuclear magnetic-resonance (COSY) - manifestation of conformational equilibria involving carboxylate groups. J Mol Biol 179:283-288
    • (1984) J Mol Biol , vol.179 , pp. 283-288
    • Ebina, S.1    Wüthrich, K.2
  • 44
    • 0020855355 scopus 로고
    • Hydrogen exchange and structural dynamics of proteins and nucleic acids
    • Englander SW, Kallenbach NR (1983) Hydrogen exchange and structural dynamics of proteins and nucleic acids. Q Rev Biophys 16:521-655
    • (1983) Q Rev Biophys , vol.16 , pp. 521-655
    • Englander, S.W.1    Kallenbach, N.R.2
  • 47
    • 67650082785 scopus 로고    scopus 로고
    • Recent advances in solution NMR: Fast methods and heteronuclear direct detection
    • Felli IC, Brutscher B (2009) Recent advances in solution NMR: fast methods and heteronuclear direct detection. ChemPhysChem 10:1356-1368
    • (2009) ChemPhysChem , vol.10 , pp. 1356-1368
    • Felli, I.C.1    Brutscher, B.2
  • 48
    • 0036099192 scopus 로고    scopus 로고
    • Experimental pKa values of buried residues: Analysis with continuum methods and role of water penetration
    • Fitch CA, Karp DA, Lee KK, Stites WE, Lattman EE, Garcia-Moreno EB (2002) Experimental pKa values of buried residues: analysis with continuum methods and role of water penetration. Biophys J 82:3289-3304
    • (2002) Biophys J , vol.82 , pp. 3289-3304
    • Fitch, C.A.1    Karp, D.A.2    Lee, K.K.3    Stites, W.E.4    Lattman, E.E.5    Garcia-Moreno, E.B.6
  • 49
    • 0026511733 scopus 로고
    • Relationship between electrostatics and redox function in human thioredoxin - Characterization of pH titration shifts using 2-dimensional homonuclear and heteronuclear NMR
    • Forman-Kay JD, Clore GM, Gronenborn AM (1992) Relationship between electrostatics and redox function in human thioredoxin - characterization of pH titration shifts using 2-dimensional homonuclear and heteronuclear NMR. Biochemistry 31:3442-3452
    • (1992) Biochemistry , vol.31 , pp. 3442-3452
    • Forman-Kay, J.D.1    Clore, G.M.2    Gronenborn, A.M.3
  • 50
    • 0036681440 scopus 로고    scopus 로고
    • Empirical relationships between protein structure and carboxyl pKa values in proteins
    • Forsyth WR, Antosiewicz JM, Robertson AD (2002) Empirical relationships between protein structure and carboxyl pKa values in proteins. Proteins Struct Func Bioinform 48:388-4034
    • (2002) Proteins Struct Func Bioinform , vol.48 , pp. 388-4034
    • Forsyth, W.R.1    Antosiewicz, J.M.2    Robertson, A.D.3
  • 52
    • 0000741348 scopus 로고    scopus 로고
    • Strong hydrogen bonding in molecules and enzymatic complexes
    • 1829524
    • Frey PA (2001) Strong hydrogen bonding in molecules and enzymatic complexes. Magn Reson Chem 39:S190-S198
    • (2001) Magn Reson Chem , vol.39 , pp. 190-S198
    • Frey, P.A.1
  • 54
    • 0018786518 scopus 로고
    • 13C nuclear magnetic resonance spectroscopy. Reaction of hen egg white lysozyme with iodoacetate
    • 13C nuclear magnetic resonance spectroscopy. Reaction of hen egg white lysozyme with iodoacetate. J Biol Chem 254:2210-2213
    • (1979) J Biol Chem , vol.254 , pp. 2210-2213
    • Goux, W.J.1    Allerhand, A.2
  • 55
    • 58149476769 scopus 로고    scopus 로고
    • A summary of the measured pK values of the ionizable groups in folded proteins
    • Grimsley GR, Scholtz JM, Pace CN (2009) A summary of the measured pK values of the ionizable groups in folded proteins. Protein Sci 18:247-251
    • (2009) Protein Sci , vol.18 , pp. 247-251
    • Grimsley, G.R.1    Scholtz, J.M.2    Pace, C.N.3
  • 56
    • 0024500323 scopus 로고
    • Staphylococcal nuclease active-site amino-acids - PH-dependence of tyrosine and arginine as determined by NMR and kinetic-studies
    • Grissom CB, Chinami MA, Benway DA, Ulrich EL, Markley JL (1987) Staphylococcal nuclease active-site amino-acids - pH-dependence of tyrosine and arginine as determined by NMR and kinetic-studies. Biochemistry 28:2116-2124
    • (1987) Biochemistry , vol.28 , pp. 2116-2124
    • Grissom, C.B.1    Chinami, M.A.2    Benway, D.A.3    Ulrich, E.L.4    Markley, J.L.5
  • 59
    • 78650899625 scopus 로고    scopus 로고
    • Hydrogen bonding in the active site of ketosteroid isomerase: Electronic inductive effects and hydrogen bond coupling
    • Hanoian P, Sigala PA, Herschlag D, Hammes-Schiffer S (2010) Hydrogen bonding in the active site of ketosteroid isomerase: electronic inductive effects and hydrogen bond coupling. Biochemistry 49:10339-10348
    • (2010) Biochemistry , vol.49 , pp. 10339-10348
    • Hanoian, P.1    Sigala, P.A.2    Herschlag, D.3    Hammes-Schiffer, S.4
  • 60
    • 49149139337 scopus 로고
    • Carbon-hydrogen spin-spin coupling-constants
    • Hansen PE (1981) Carbon-hydrogen spin-spin coupling-constants. Prog Nucl Magn Reson Spect 14:175-296
    • (1981) Prog Nucl Magn Reson Spect , vol.14 , pp. 175-296
    • Hansen, P.E.1
  • 61
    • 0033622401 scopus 로고    scopus 로고
    • Isotope effects on chemical shifts of proteins and peptides
    • Hansen PE (2000) Isotope effects on chemical shifts of proteins and peptides. Magn Reson Chem 38:1-10
    • (2000) Magn Reson Chem , vol.38 , pp. 1-10
    • Hansen, P.E.1
  • 62
    • 38349042050 scopus 로고    scopus 로고
    • Isotope effect on chemical shifts in hydrogen-bonded systems
    • Hansen PE (2007) Isotope effect on chemical shifts in hydrogen-bonded systems. J Labelled Compd Rad 50:967-981
    • (2007) J Labelled Compd Rad , vol.50 , pp. 967-981
    • Hansen, P.E.1
  • 63
    • 84899622622 scopus 로고    scopus 로고
    • Measurement of histidine pKa values and tautomer populations in invisible protein states
    • 2014PNAS.111E1705H
    • Hansen AL, Kay LE (2014) Measurement of histidine pKa values and tautomer populations in invisible protein states. Proc Natl Acad Sci U S A 111:E1705-E1712
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. 1705-E1712
    • Hansen, A.L.1    Kay, L.E.2
  • 64
    • 0001475636 scopus 로고
    • A reinvestigation of one-bond deuterium-isotope effects on nitrogen and on proton nuclear shielding for the ammonium ion
    • Hansen PE, Lycka A (1989) A reinvestigation of one-bond deuterium-isotope effects on nitrogen and on proton nuclear shielding for the ammonium ion. Acta Chem Scand 43:222-232
    • (1989) Acta Chem Scand , vol.43 , pp. 222-232
    • Hansen, P.E.1    Lycka, A.2
  • 65
    • 81055154363 scopus 로고    scopus 로고
    • Arginine residues at internal positions in a protein are always charged
    • 2011PNAS.10818954H
    • Harms MJ, Schlessman JL, Sue GR, Garcia-Moreno B (2011) Arginine residues at internal positions in a protein are always charged. Proc Natl Acad Sci USA 108:18954-18959
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 18954-18959
    • Harms, M.J.1    Schlessman, J.L.2    Sue, G.R.3    Garcia-Moreno, B.4
  • 66
    • 0036001159 scopus 로고    scopus 로고
    • Structural basis of perturbed pKa values of catalytic groups in enzyme active sites
    • Harris TK, Turner GJ (2002) Structural basis of perturbed pKa values of catalytic groups in enzyme active sites. IUBMB life 53:85-98
    • (2002) IUBMB Life , vol.53 , pp. 85-98
    • Harris, T.K.1    Turner, G.J.2
  • 67
    • 0024393437 scopus 로고
    • 1H nuclear magnetic resonance measurements of amide proton exchange rates and pH-dependent chemical shifts
    • 1H nuclear magnetic resonance measurements of amide proton exchange rates and pH-dependent chemical shifts. Biochemistry 28:4312-4317
    • (1989) Biochemistry , vol.28 , pp. 4312-4317
    • Haruyama, H.1    Qian, Y.Q.2    Wüthrich, K.3
  • 68
    • 44949260034 scopus 로고    scopus 로고
    • Probing electric fields in proteins in solution by NMR spectroscopy
    • Hass MA, Jensen MR, Led JJ (2008) Probing electric fields in proteins in solution by NMR spectroscopy. Proteins 72:333-343
    • (2008) Proteins , vol.72 , pp. 333-343
    • Hass, M.A.1    Jensen, M.R.2    Led, J.J.3
  • 69
    • 0025365762 scopus 로고
    • 15N NMR spectroscopy - Use of the INEPT experiment to follow individual amides in detergent-solubilized M13 coat protein
    • 15N NMR spectroscopy - use of the INEPT experiment to follow individual amides in detergent-solubilized M13 coat protein. Biochemistry 29:6303-6313
    • (1990) Biochemistry , vol.29 , pp. 6303-6313
    • Henry, G.D.1    Sykes, B.D.2
  • 70
    • 34249757710 scopus 로고
    • Determination of the rotational-dynamics and pH-dependence of the hydrogen-exchange rates of the arginine guanidino group using NMR spectroscopy
    • Henry GD, Sykes BD (1995) Determination of the rotational-dynamics and pH-dependence of the hydrogen-exchange rates of the arginine guanidino group using NMR spectroscopy. J Biomol NMR 6:59-66
    • (1995) J Biomol NMR , vol.6 , pp. 59-66
    • Henry, G.D.1    Sykes, B.D.2
  • 73
    • 0015866169 scopus 로고
    • Carbon nuclear magnetic-resonance studies of histidine residue in alpha-lytic protease - Implications for catalytic mechanism of serine proteases
    • Hunkapiler MW, Smallcombe SH, Whitaker DR, Richards JH (1973) Carbon nuclear magnetic-resonance studies of histidine residue in alpha-lytic protease - implications for catalytic mechanism of serine proteases. Biochemistry 12:4732-4743
    • (1973) Biochemistry , vol.12 , pp. 4732-4743
    • Hunkapiler, M.W.1    Smallcombe, S.H.2    Whitaker, D.R.3    Richards, J.H.4
  • 74
    • 0033783910 scopus 로고    scopus 로고
    • Evidence for a perturbation of arginine-82 in the bacteriorhodopsin photocycle from time-resolved infrared spectra
    • Hutson MS, Alexiev U, Shilov SV, Wise KJ, Braiman MS (2000) Evidence for a perturbation of arginine-82 in the bacteriorhodopsin photocycle from time-resolved infrared spectra. Biochemistry 39:13189-13200
    • (2000) Biochemistry , vol.39 , pp. 13189-13200
    • Hutson, M.S.1    Alexiev, U.2    Shilov, S.V.3    Wise, K.J.4    Braiman, M.S.5
  • 78
    • 0029057023 scopus 로고
    • Proton sharing between cysteine thiols in Escherichia coli thioredoxin - Implications for the mechanism of protein disulfide reduction
    • Jeng MF, Holmgren A, Dyson HJ (1995) Proton sharing between cysteine thiols in Escherichia coli thioredoxin - implications for the mechanism of protein disulfide reduction. Biochemistry 34:10101-10105
    • (1995) Biochemistry , vol.34 , pp. 10101-10105
    • Jeng, M.F.1    Holmgren, A.2    Dyson, H.J.3
  • 79
    • 0031283399 scopus 로고    scopus 로고
    • Complete measurement of the pKa values of the carboxyl and imidazole groups in Bacillus circulans xylanase
    • Joshi MD, Hedberg A, McIntosh LP (1997) Complete measurement of the pKa values of the carboxyl and imidazole groups in Bacillus circulans xylanase. Protein Sci 6:2667-2670
    • (1997) Protein Sci , vol.6 , pp. 2667-2670
    • Joshi, M.D.1    Hedberg, A.2    McIntosh, L.P.3
  • 80
    • 0034716940 scopus 로고    scopus 로고
    • Hydrogen bonding and catalysis: A novel explanation for how a single amino acid substitution can change the pH optimum of a glycosidase
    • Joshi MD, Sidhu G, Pot I, Brayer GD, Withers SG, McIntosh LP (2000) Hydrogen bonding and catalysis: a novel explanation for how a single amino acid substitution can change the pH optimum of a glycosidase. J Mol Biol 299:255-279
    • (2000) J Mol Biol , vol.299 , pp. 255-279
    • Joshi, M.D.1    Sidhu, G.2    Pot, I.3    Brayer, G.D.4    Withers, S.G.5    McIntosh, L.P.6
  • 82
    • 0020782070 scopus 로고
    • 15N NMR study of the barriers to isomerization about guanidinium and guanidino carbon nitrogen bonds in L-arginine
    • 15N NMR study of the barriers to isomerization about guanidinium and guanidino carbon nitrogen bonds in L-arginine. J Am Chem Soc 105:4698-4701
    • (1983) J Am Chem Soc , vol.105 , pp. 4698-4701
    • Kanamori, K.1    Roberts, J.D.2
  • 84
    • 0343778162 scopus 로고
    • Nitrogen-15 nuclear magnetic-resonance of histidine - Effect of pH
    • Kawano K, Kyogoku Y (1975) Nitrogen-15 nuclear magnetic-resonance of histidine - effect of pH. Chem Lett 12:1305-1308
    • (1975) Chem Lett , vol.12 , pp. 1305-1308
    • Kawano, K.1    Kyogoku, Y.2
  • 86
    • 0015766825 scopus 로고
    • 13C nuclear magnetic-resonance of pentapeptides of glycine containing central residues of serine, threonine, aspartic and glutamic acids, asparagine, and glutamin
    • 13C nuclear magnetic-resonance of pentapeptides of glycine containing central residues of serine, threonine, aspartic and glutamic acids, asparagine, and glutamin. J Biol Chem 248:7811-7818
    • (1973) J Biol Chem , vol.248 , pp. 7811-7818
    • Keim, P.1    Vigna, R.A.2    Morrow, J.S.3    Marshall, R.C.4    Gurd, F.R.N.5
  • 87
    • 0016187781 scopus 로고
    • 13C nuclear magnetic-resonance of pentapeptides of glycine containing central residues of methionine, proline, arginine, and lysine
    • 13C nuclear magnetic-resonance of pentapeptides of glycine containing central residues of methionine, proline, arginine, and lysine. J Biol Chem 249:4149-4156
    • (1974) J Biol Chem , vol.249 , pp. 4149-4156
    • Keim, P.1    Vigna, R.A.2    Nigen, A.M.3    Morrow, J.S.4    Gurd, F.R.N.5
  • 88
    • 0030596490 scopus 로고    scopus 로고
    • Measurement and modelling of sequence-specific pKa values of lysine residues in calbindin D9k
    • Kesvatera T, Jonsson B, Thulin E, Linse S (1996) Measurement and modelling of sequence-specific pKa values of lysine residues in calbindin D9k. J Mol Biol 259:828-839
    • (1996) J Mol Biol , vol.259 , pp. 828-839
    • Kesvatera, T.1    Jonsson, B.2    Thulin, E.3    Linse, S.4
  • 89
    • 0030610243 scopus 로고    scopus 로고
    • PKa 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
    • Khare D, Alexander P, Antosiewicz J, Bryan P, Gilson M, Orban J (1997) pKa 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
    • (1997) Biochemistry , vol.36 , pp. 3580-3589
    • Khare, D.1    Alexander, P.2    Antosiewicz, J.3    Bryan, P.4    Gilson, M.5    Orban, J.6
  • 90
    • 79954427635 scopus 로고    scopus 로고
    • Random coil chemical shift for intrinsically disordered proteins: Effects of temperature and pH
    • Kjaergaard M, Brander S, Poulsen FM (2011) Random coil chemical shift for intrinsically disordered proteins: effects of temperature and pH. J Biomol NMR 49:139-149
    • (2011) J Biomol NMR , vol.49 , pp. 139-149
    • Kjaergaard, M.1    Brander, S.2    Poulsen, F.M.3
  • 91
    • 0017018406 scopus 로고
    • The intrinsic pKa values of functional groups in enzymes: Improper deductions from the pH-dependence of steady-state parameters
    • Knowles JR (1976) The intrinsic pKa values of functional groups in enzymes: improper deductions from the pH-dependence of steady-state parameters. CRC Crit Rev Biochem 4:165-173
    • (1976) CRC Crit Rev Biochem , vol.4 , pp. 165-173
    • Knowles, J.R.1
  • 94
    • 77949314365 scopus 로고    scopus 로고
    • Improving the analysis of NMR spectra tracking pH-induced conformational changes: Removing artefacts of the electric field on the NMR chemical shift
    • Kukic P, Farrell D, Søndergaard CR, Bjarnadottir U, Bradley J, Pollastri G, Nielsen JE (2010) Improving the analysis of NMR spectra tracking pH-induced conformational changes: removing artefacts of the electric field on the NMR chemical shift. Proteins Struct Func Bioinform 78:971-984
    • (2010) Proteins Struct Func Bioinform , vol.78 , pp. 971-984
    • Kukic, P.1    Farrell, D.2    Søndergaard, C.R.3    Bjarnadottir, U.4    Bradley, J.5    Pollastri, G.6    Nielsen, J.E.7
  • 95
    • 84887794679 scopus 로고    scopus 로고
    • Protein dielectric constants determined from NMR chemical shift perturbations
    • Kukic P et al (2013) Protein dielectric constants determined from NMR chemical shift perturbations. J Am Chem Soc 135:16968-16976
    • (2013) J Am Chem Soc , vol.135 , pp. 16968-16976
    • Kukic, P.1
  • 96
    • 49549145980 scopus 로고
    • 13C chemical shifts in amino acids and dipeptides
    • 1975JMagR.20.530K
    • 13C chemical shifts in amino acids and dipeptides. J Magn Reson 20:530-534
    • (1975) J Magn Reson , vol.20 , pp. 530-534
    • Ladner, H.K.1    Led, J.J.2    Grant, D.M.3
  • 97
    • 47749114186 scopus 로고    scopus 로고
    • Short strong hydrogen bonds in proteins: A case study of rhamnogalacturonan acetylesterase
    • Langkilde A et al (2008) Short strong hydrogen bonds in proteins: a case study of rhamnogalacturonan acetylesterase. Acta Crystallogr D 64:851-863
    • (2008) Acta Crystallogr D , vol.64 , pp. 851-863
    • Langkilde, A.1
  • 98
    • 84867668538 scopus 로고    scopus 로고
    • The PNT domain from Drosophila Pointed-P2 contains a dynamic N-terminal helix preceded by a disordered phosphoacceptor sequence
    • Lau DKW, Okon M, McIntosh LP (2012) The PNT domain from Drosophila Pointed-P2 contains a dynamic N-terminal helix preceded by a disordered phosphoacceptor sequence. Protein Sci 21:1716-1725
    • (2012) Protein Sci , vol.21 , pp. 1716-1725
    • Lau, D.K.W.1    Okon, M.2    McIntosh, L.P.3
  • 99
    • 42449094180 scopus 로고    scopus 로고
    • Ultrahigh-resolution crystallography and related electron density and electrostatic properties in proteins
    • Lecomte C, Jelsch C, Guillot B, Fournier B, Lagoutte A (2008) Ultrahigh-resolution crystallography and related electron density and electrostatic properties in proteins. J Synchrotron Rad 15:202-203
    • (2008) J Synchrotron Rad , vol.15 , pp. 202-203
    • Lecomte, C.1    Jelsch, C.2    Guillot, B.3    Fournier, B.4    Lagoutte, A.5
  • 100
    • 0000401116 scopus 로고
    • 13C chemical-shifts in selected amino-acids as function of pH
    • 1979JMagR.33.603L
    • 13C chemical-shifts in selected amino-acids as function of pH. J Magn Reson 33:603-6170
    • (1979) J Magn Reson , vol.33 , pp. 603-6170
    • Led, J.J.1    Petersen, S.B.2
  • 102
    • 79551714030 scopus 로고    scopus 로고
    • Protonation, tautomerization, and rotameric structure of histidine: A comprehensive study by magic-angle-spinning solid-state NMR
    • Li SH, Hong M (2011) Protonation, tautomerization, and rotameric structure of histidine: a comprehensive study by magic-angle-spinning solid-state NMR. J Am Chem Soc 133:1534-1544
    • (2011) J Am Chem Soc , vol.133 , pp. 1534-1544
    • Li, S.H.1    Hong, M.2
  • 103
    • 33845378767 scopus 로고
    • PH measurement in concentrated alkaline-solutions
    • Licht S (1985) pH measurement in concentrated alkaline-solutions. Anal Chem 57:514-519
    • (1985) Anal Chem , vol.57 , pp. 514-519
    • Licht, S.1
  • 104
    • 0030051552 scopus 로고    scopus 로고
    • Proton exchange rates from amino acid side chains - Implications for image contrast
    • Liepinsh E, Otting G (1996) Proton exchange rates from amino acid side chains - implications for image contrast. Magn Reson Med 35:30-42
    • (1996) Magn Reson Med , vol.35 , pp. 30-42
    • Liepinsh, E.1    Otting, G.2
  • 105
    • 0026925802 scopus 로고
    • NMR spectroscopy of hydroxyl protons in aqueous solutions of peptides and proteins
    • Liepinsh E, Otting G, Wüthrich K (1992) NMR spectroscopy of hydroxyl protons in aqueous solutions of peptides and proteins. J Biomol NMR 2:447-465
    • (1992) J Biomol NMR , vol.2 , pp. 447-465
    • Liepinsh, E.1    Otting, G.2    Wüthrich, K.3
  • 106
    • 84864092960 scopus 로고    scopus 로고
    • A low pKa cysteine at the active site of mouse methionine sulfoxide reductase A
    • Lim JC, Gruschus JM, Kim G, Berlett BS, Tjandra N, Levine RL (2012) A low pKa cysteine at the active site of mouse methionine sulfoxide reductase A. J Biol Chem 287:25596-25601
    • (2012) J Biol Chem , vol.287 , pp. 25596-25601
    • Lim, J.C.1    Gruschus, J.M.2    Kim, G.3    Berlett, B.S.4    Tjandra, N.5    Levine, R.L.6
  • 107
    • 33751560650 scopus 로고    scopus 로고
    • Electrostatic contributions to residue-specific protonation equilibria and proton binding capacitance for a small protein
    • Lindman S, Linse S, Mulder FA, Andre I (2006) Electrostatic contributions to residue-specific protonation equilibria and proton binding capacitance for a small protein. Biochemistry 45:13993-14002
    • (2006) Biochemistry , vol.45 , pp. 13993-14002
    • Lindman, S.1    Linse, S.2    Mulder, F.A.3    Andre, I.4
  • 108
    • 33846011386 scopus 로고    scopus 로고
    • PKa values for side-chain carboxyl groups of a PGB1 variant explain salt and pH-dependent stability
    • Lindman S, Linse S, Mulder FA, Andre I (2007) pKa values for side-chain carboxyl groups of a PGB1 variant explain salt and pH-dependent stability. Biophys J 92:257-266
    • (2007) Biophys J , vol.92 , pp. 257-266
    • Lindman, S.1    Linse, S.2    Mulder, F.A.3    Andre, I.4
  • 110
    • 27244451944 scopus 로고    scopus 로고
    • Triple-resonance methods for complete resonance assignment of aromatic protons and directly bound heteronuclei in histidine and tryptophan residues
    • Löhr F, Rogov VV, Shi MC, Bernhard F, Dötsch V (2005) Triple-resonance methods for complete resonance assignment of aromatic protons and directly bound heteronuclei in histidine and tryptophan residues. J Biomol NMR 32:309-328
    • (2005) J Biomol NMR , vol.32 , pp. 309-328
    • Löhr, F.1    Rogov, V.V.2    Shi, M.C.3    Bernhard, F.4    Dötsch, V.5
  • 111
    • 0040777840 scopus 로고
    • Correlation of carboxyl carbon titration shifts and pK values
    • 1980JMagR.38.173L
    • London RE (1980) Correlation of carboxyl carbon titration shifts and pK values. J Magn Reson 38:173-177
    • (1980) J Magn Reson , vol.38 , pp. 173-177
    • London, R.E.1
  • 114
    • 84877356787 scopus 로고    scopus 로고
    • Strategies for modulating the pH-dependent activity of a family 11 glycoside hydrolase
    • Ludwiczek ML et al (2013) Strategies for modulating the pH-dependent activity of a family 11 glycoside hydrolase. Biochemistry 52:3138-3156
    • (2013) Biochemistry , vol.52 , pp. 3138-3156
    • Ludwiczek, M.L.1
  • 115
    • 0002870406 scopus 로고
    • Observation of histidine residues in proteins by means of nuclear magnetic-resonance spectroscopy
    • Markley JL (1975) Observation of histidine residues in proteins by means of nuclear magnetic-resonance spectroscopy. Acc Chem Res 8:70-80
    • (1975) Acc Chem Res , vol.8 , pp. 70-80
    • Markley, J.L.1
  • 116
    • 34249936136 scopus 로고    scopus 로고
    • Active-site properties of the oxidized and reduced C-terminal domain of DsbD obtained by NMR spectroscopy
    • Mavridou DAI, Stevens JM, Ferguson SJ, Redfield C (2007) Active-site properties of the oxidized and reduced C-terminal domain of DsbD obtained by NMR spectroscopy. J Mol Biol 370:643-658
    • (2007) J Mol Biol , vol.370 , pp. 643-658
    • Mavridou, D.A.I.1    Stevens, J.M.2    Ferguson, S.J.3    Redfield, C.4
  • 117
    • 84985694498 scopus 로고
    • Side chain-backbone hydrogen-bonds in peptides containing glutamic-acid residues
    • Mayer R, Lancelot G, Spach G (1979) Side chain-backbone hydrogen-bonds in peptides containing glutamic-acid residues. Biopolymers 18:1293-1296
    • (1979) Biopolymers , vol.18 , pp. 1293-1296
    • Mayer, R.1    Lancelot, G.2    Spach, G.3
  • 119
    • 0029666454 scopus 로고    scopus 로고
    • 13C-NMR study of Bacillus circulans xylanase
    • 13C-NMR study of Bacillus circulans xylanase. Biochemistry 35:9958-9966
    • (1996) Biochemistry , vol.35 , pp. 9958-9966
    • McIntosh, L.P.1
  • 121
    • 80755187569 scopus 로고    scopus 로고
    • Dissecting electrostatic interactions in Bacillus circulans xylanase through NMR-monitored pH titrations
    • 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 51:5-19
    • (2011) J Biomol NMR , vol.51 , pp. 5-19
    • McIntosh, L.P.1    Naito, D.2    Baturin, S.J.3    Okon, M.4    Joshi, M.D.5    Nielsen, J.E.6
  • 122
    • 11144354250 scopus 로고    scopus 로고
    • FTIR studies of internal proton transfer reactions linked to inter-heme electron transfer in bovine cytochrome c oxidase
    • McMahon BH et al (2004) FTIR studies of internal proton transfer reactions linked to inter-heme electron transfer in bovine cytochrome c oxidase. Biochim Biophys Acta 1655:321-331
    • (2004) Biochim Biophys Acta , vol.1655 , pp. 321-331
    • McMahon, B.H.1
  • 123
    • 84904294389 scopus 로고    scopus 로고
    • 13C solid-state NMR spectroscopy
    • 2014JMagR.245.105M
    • 13C solid-state NMR spectroscopy. J Magn Reson 245C:105-109
    • (2014) J Magn Reson , vol.245 , pp. 105-109
    • Miao, Y.1    Cross, T.A.2    Fu, R.3
  • 124
    • 4243518910 scopus 로고    scopus 로고
    • Influence of the pKa value of the buried, active-site cysteine on the redox properties of thioredoxin-like oxidoreductases
    • Mossner E, Iwai H, Glockshuber R (2000) Influence of the pKa value of the buried, active-site cysteine on the redox properties of thioredoxin-like oxidoreductases. FEBS Lett 477:21-26
    • (2000) FEBS Lett , vol.477 , pp. 21-26
    • Mossner, E.1    Iwai, H.2    Glockshuber, R.3
  • 126
    • 81055156704 scopus 로고    scopus 로고
    • The pKa Cooperative: A collaborative effort to advance structure-based calculations of pKa values and electrostatic effects in proteins
    • Nielsen JE, Gunner MR, Garcia-Moreno BE (2011) The pKa Cooperative: a collaborative effort to advance structure-based calculations of pKa values and electrostatic effects in proteins. Proteins 79:3249-3259
    • (2011) Proteins , vol.79 , pp. 3249-3259
    • Nielsen, J.E.1    Gunner, M.R.2    Garcia-Moreno, B.E.3
  • 127
    • 37549049041 scopus 로고    scopus 로고
    • Neutron protein crystallography: Beyond the folding structure of biological macromolecules
    • 2008AcCrA.64.12N
    • Niimura N, Bau R (2008) Neutron protein crystallography: beyond the folding structure of biological macromolecules. Acta Cryst Section A 64:12-22
    • (2008) Acta Cryst Section A , vol.64 , pp. 12-22
    • Niimura, N.1    Bau, R.2
  • 128
    • 33750429700 scopus 로고    scopus 로고
    • Intrinsic relative stabilities of the neutral tautomers of arginine side-chain models
    • Norberg J, Foloppe N, Nilsson L (2005) Intrinsic relative stabilities of the neutral tautomers of arginine side-chain models. J Chem Theory Comput 1:986-993
    • (2005) J Chem Theory Comput , vol.1 , pp. 986-993
    • Norberg, J.1    Foloppe, N.2    Nilsson, L.3
  • 129
    • 0032959801 scopus 로고    scopus 로고
    • Direct NMR observation of the Cys-14 thiol proton of reduced Escherichia coli glutaredoxin-3 supports the presence of an active site thiol-thiolate hydrogen bond
    • Nordstrand K, Aslund F, Meunier S, Holmgren A, Otting G, Berndt KD (1999) Direct NMR observation of the Cys-14 thiol proton of reduced Escherichia coli glutaredoxin-3 supports the presence of an active site thiol-thiolate hydrogen bond. FEBS Lett 449:196-200
    • (1999) FEBS Lett , vol.449 , pp. 196-200
    • Nordstrand, K.1    Aslund, F.2    Meunier, S.3    Holmgren, A.4    Otting, G.5    Berndt, K.D.6
  • 130
    • 37049140963 scopus 로고
    • 13C nuclear magnetic-resonance study of tyrosine titrations
    • 13C nuclear magnetic-resonance study of tyrosine titrations. J Chem Soc Chem Comm 21:870-871
    • (1974) J Chem Soc Chem Comm , vol.21 , pp. 870-871
    • Norton, R.S.1    Bradbury, J.H.2
  • 131
    • 0028232021 scopus 로고
    • Individual ionization-constants of all the carboxyl groups in ribonuclease HI from Escherichia coli determined by NMR
    • Oda Y, Yamazaki T, Nagayama K, Kanaya S, Kuroda Y, Nakamura H (1994) Individual ionization-constants of all the carboxyl groups in ribonuclease HI from Escherichia coli determined by NMR. Biochemistry 33:5275-5284
    • (1994) Biochemistry , vol.33 , pp. 5275-5284
    • Oda, Y.1    Yamazaki, T.2    Nagayama, K.3    Kanaya, S.4    Kuroda, Y.5    Nakamura, H.6
  • 133
    • 0016825166 scopus 로고
    • Studies of individual carbon sites of proteins in solution by natural abundance carbon 13 nuclear magnetic-resonance spectroscopy - Relaxation behavior
    • Oldfield E, Norton RS, Allerhand A (1975a) 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
  • 134
    • 0016840028 scopus 로고
    • Studies of individual carbon sites of proteins in solution by natural abundance carbon 13 nuclear magnetic-resonance spectroscopy - Strategies for assignments
    • Oldfield E, Norton RS, Allerhand A (1975b) 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
  • 135
    • 0015522917 scopus 로고
    • Ionization behavior of the catalytic carboxyls of lysozyme. Effects of ionic strength
    • Parsons SM, Raftery MA (1972) Ionization behavior of the catalytic carboxyls of lysozyme. Effects of ionic strength. Biochemistry 11:1623-1629
    • (1972) Biochemistry , vol.11 , pp. 1623-1629
    • Parsons, S.M.1    Raftery, M.A.2
  • 137
    • 0027456412 scopus 로고
    • 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
    • Pelton JG, Torchia DA, Meadow ND, Roseman S (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. Protein Sci 2:543-558
    • (1993) Protein Sci , vol.2 , pp. 543-558
    • Pelton, J.G.1    Torchia, D.A.2    Meadow, N.D.3    Roseman, S.4
  • 138
    • 0033514389 scopus 로고    scopus 로고
    • Arginine activity in the proton-motive photocycle of bacteriorhodopsin: Solid-state NMR studies of the wild-type and D85N proteins
    • Petkova AT, Hu JG, Bizounok M, Simpson M, Griffin RG, Herzfeld J (1999) Arginine activity in the proton-motive photocycle of bacteriorhodopsin: solid-state NMR studies of the wild-type and D85N proteins. Biochemistry 38:1562-1572
    • (1999) Biochemistry , vol.38 , pp. 1562-1572
    • Petkova, A.T.1    Hu, J.G.2    Bizounok, M.3    Simpson, M.4    Griffin, R.G.5    Herzfeld, J.6
  • 139
    • 0029843569 scopus 로고    scopus 로고
    • Characterization of a buried neutral histidine residue in Bacillus circulans xylanase: NMR assignments, pH titration, and hydrogen exchange
    • Plesniak LA, Connelly GP, Wakarchuk WW, McIntosh LP (1996) Characterization of a buried neutral histidine residue in Bacillus circulans xylanase: NMR assignments, pH titration, and hydrogen exchange. Protein Sci 5:2319-2328
    • (1996) Protein Sci , vol.5 , pp. 2319-2328
    • Plesniak, L.A.1    Connelly, G.P.2    Wakarchuk, W.W.3    McIntosh, L.P.4
  • 141
    • 33645228911 scopus 로고    scopus 로고
    • Guidelines for NMR measurements for determination of high and low pKa values
    • Popov K, Ronkkomaki H, Lajunen LHJ (2006) Guidelines for NMR measurements for determination of high and low pKa values. Pure Appl Chem 78:663-675
    • (2006) Pure Appl Chem , vol.78 , pp. 663-675
    • Popov, K.1    Ronkkomaki, H.2    Lajunen, L.H.J.3
  • 145
    • 33746047069 scopus 로고    scopus 로고
    • The pH-dependence of amide chemical shift of Asp/Glu reflects its pKa in intrinsically disordered proteins with only local interactions
    • Pujato M, Navarro A, Versace R, Mancusso R, Ghose R, Tasayco ML (2006) The pH-dependence of amide chemical shift of Asp/Glu reflects its pKa in intrinsically disordered proteins with only local interactions. BBA-Proteins Proteom 1764:1227-1233
    • (2006) BBA-Proteins Proteom , vol.1764 , pp. 1227-1233
    • Pujato, M.1    Navarro, A.2    Versace, R.3    Mancusso, R.4    Ghose, R.5    Tasayco, M.L.6
  • 147
    • 0008632507 scopus 로고
    • 13C chemical shift parameters for amines, carboxylic acids, and amino acids
    • 1976JMagR.24.27R
    • 13C chemical shift parameters for amines, carboxylic acids, and amino acids. J Magn Reson 24:27-39
    • (1976) J Magn Reson , vol.24 , pp. 27-39
    • Rabenstein, D.L.1    Sayer, T.L.2
  • 148
    • 0001374747 scopus 로고
    • Determination of microscopic acid dissociation constants by nuclear magnetic-resonance spectrometry
    • Rabenstein DL, Sayer TL (1976b) Determination of microscopic acid dissociation constants by nuclear magnetic-resonance spectrometry. Anal Chem 48:1141-1145
    • (1976) Anal Chem , vol.48 , pp. 1141-1145
    • Rabenstein, D.L.1    Sayer, T.L.2
  • 149
    • 0037314994 scopus 로고    scopus 로고
    • Consequences of proton transfer in guanidine
    • Raczynska ED et al (2003) Consequences of proton transfer in guanidine. J Phys Org Chem 16:91-106
    • (2003) J Phys Org Chem , vol.16 , pp. 91-106
    • Raczynska, E.D.1
  • 150
    • 0028589065 scopus 로고
    • Structural consequences of histidine phosphorylation - NMR characterization of the phosphohistidine form of histidine-containing protein from Bacillus subtilis and Escherichia coli
    • Rajagopal P, Waygood EB, Klevit RE (1994) Structural consequences of histidine phosphorylation - NMR characterization of the phosphohistidine form of histidine-containing protein from Bacillus subtilis and Escherichia coli. Biochemistry 33:15271-15282
    • (1994) Biochemistry , vol.33 , pp. 15271-15282
    • Rajagopal, P.1    Waygood, E.B.2    Klevit, R.E.3
  • 154
    • 1642300619 scopus 로고
    • Nitrogen-14 nuclear magnetic-resonance study of amino acids, peptides, and other biologically interesting molecules
    • Richards RE, Thomas NA (1974) Nitrogen-14 nuclear magnetic-resonance study of amino acids, peptides, and other biologically interesting molecules. J Chem Soc Perk T 2:368-374
    • (1974) J Chem Soc Perk T , vol.2 , pp. 368-374
    • Richards, R.E.1    Thomas, N.A.2
  • 155
    • 0018118592 scopus 로고
    • 13C NMR chemical-shifts of common amino acid residues measured in aqueous-solutions of linear tetrapeptides H-Gly-Gly-X-L-Ala-OH
    • 13C NMR chemical-shifts of common amino acid residues measured in aqueous-solutions of linear tetrapeptides H-Gly-Gly-X-L-Ala-OH. Biopolymers 17:2133-2141
    • (1978) Biopolymers , vol.17 , pp. 2133-2141
    • Richarz, R.1    Wüthrich, K.2
  • 156
    • 0000762203 scopus 로고
    • 15N nuclear magnetic-resonance study of the acid-base and tautomeric equilibria of 4-substituted imidazoles and its relevance to the catalytic mechanism of α-lytic protease
    • 15N nuclear magnetic-resonance study of the acid-base and tautomeric equilibria of 4-substituted imidazoles and its relevance to the catalytic mechanism of α-lytic protease. J Am Chem Soc 104:3945-3949
    • (1982) J Am Chem Soc , vol.104 , pp. 3945-3949
    • Roberts, J.D.1    Yu, C.2    Flanagan, C.3    Birdseye, T.R.4
  • 157
    • 0015506470 scopus 로고
    • High-resolution nuclear magnetic-resonance study of histidine - Aspartate hydrogen-bond in chymotrypsin and chymotrypsinogen
    • Robillard G, Shulman RG (1972) High-resolution nuclear magnetic-resonance study of histidine - aspartate hydrogen-bond in chymotrypsin and chymotrypsinogen. J Mol Biol 71:507-511
    • (1972) J Mol Biol , vol.71 , pp. 507-511
    • Robillard, G.1    Shulman, R.G.2
  • 158
    • 84868206533 scopus 로고    scopus 로고
    • Understanding the pKa of redox cysteines: The key role of hydrogen bonding
    • Roos G, Foloppe N, Messens J (2013) Understanding the pKa of redox cysteines: the key role of hydrogen bonding. Antioxid Redox Sign 18:94-127
    • (2013) Antioxid Redox Sign , vol.18 , pp. 94-127
    • Roos, G.1    Foloppe, N.2    Messens, J.3
  • 159
    • 84856811500 scopus 로고    scopus 로고
    • H atom positions and nuclear magnetic resonance chemical shifts of short H bonds in photoactive yellow protein
    • Saito K, Ishikita H (2012) H atom positions and nuclear magnetic resonance chemical shifts of short H bonds in photoactive yellow protein. Biochemistry 51:1171-1177
    • (2012) Biochemistry , vol.51 , pp. 1171-1177
    • Saito, K.1    Ishikita, H.2
  • 160
    • 0347722841 scopus 로고    scopus 로고
    • Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients
    • Sattler M, Schleucher J, Griesinger C (1999) Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients. Prog Nucl Mag Reson Specty 34:93-158
    • (1999) Prog Nucl Mag Reson Specty , vol.34 , pp. 93-158
    • Sattler, M.1    Schleucher, J.2    Griesinger, C.3
  • 161
    • 0028951968 scopus 로고
    • PH, ionic strength, and temperature dependences of ionization equilibria for the carboxyl groups in turkey ovomucoid third domain
    • Schaller W, Robertson AD (1995) pH, ionic strength, and temperature dependences of ionization equilibria for the carboxyl groups in turkey ovomucoid third domain. Biochemistry 34:4714-4723
    • (1995) Biochemistry , vol.34 , pp. 4714-4723
    • Schaller, W.1    Robertson, A.D.2
  • 162
    • 84989040610 scopus 로고
    • 31P nuclear magnetic-resonance spectroscopy of the phosphorylated tetrapeptide Gly-Gly-Asp-Ala
    • 31P nuclear magnetic-resonance spectroscopy of the phosphorylated tetrapeptide Gly-Gly-Asp-Ala. Magn Reson Chem 26:260-263
    • (1988) Magn Reson Chem , vol.26 , pp. 260-263
    • Schlemmer, H.1    Sontheimer, G.M.2    Kalbitzer, H.R.3
  • 163
    • 9744226460 scopus 로고    scopus 로고
    • A twisted base? the role of arginine in enzyme-catalyzed proton abstractions
    • Schlippe YVG, Hedstrom L (2005) A twisted base? The role of arginine in enzyme-catalyzed proton abstractions. Arch Biochem Biophys 433:266-278
    • (2005) Arch Biochem Biophys , vol.433 , pp. 266-278
    • Schlippe, Y.V.G.1    Hedstrom, L.2
  • 164
    • 34250823484 scopus 로고    scopus 로고
    • Probing electrostatic interactions along the reaction pathway of a glycoside hydrolase: Histidine characterization by NMR spectroscopy
    • Schubert M et al (2007) Probing electrostatic interactions along the reaction pathway of a glycoside hydrolase: histidine characterization by NMR spectroscopy. Biochemistry 46:7383-7395
    • (2007) Biochemistry , vol.46 , pp. 7383-7395
    • Schubert, M.1
  • 166
    • 40949101399 scopus 로고    scopus 로고
    • Exchange rate constants of invisible protons in proteins determined by NMR spectroscopy
    • Segawa T, Kateb F, Duma L, Bodenhausen G, Pelupessy P (2008) Exchange rate constants of invisible protons in proteins determined by NMR spectroscopy. ChemBioChem 9:537-542
    • (2008) ChemBioChem , vol.9 , pp. 537-542
    • Segawa, T.1    Kateb, F.2    Duma, L.3    Bodenhausen, G.4    Pelupessy, P.5
  • 167
    • 0032576146 scopus 로고    scopus 로고
    • Determination of protonation and deprotonation forms and tautomeric states of histidine residues in large proteins using nitrogen-carbon J couplings in imidazole ring
    • Shimba N, Takahashi H, Sakakura M, Fujii I, Shimada I (1998) Determination of protonation and deprotonation forms and tautomeric states of histidine residues in large proteins using nitrogen-carbon J couplings in imidazole ring. J Am Chem Soc 120:10988-10989
    • (1998) J Am Chem Soc , vol.120 , pp. 10988-10989
    • Shimba, N.1    Takahashi, H.2    Sakakura, M.3    Fujii, I.4    Shimada, I.5
  • 168
    • 0015507243 scopus 로고
    • Nuclear magnetic-resonance titration curves of histidine ring protons.2. Mathematical models for interacting groups in nuclear magnetic-resonance titration curves
    • Shrager RI, Sachs DH, Schechte A, Cohen JS, Heller SR (1972) Nuclear magnetic-resonance titration curves of histidine ring protons.2. Mathematical models for interacting groups in nuclear magnetic-resonance titration curves. Biochemistry 11:541-547
    • (1972) Biochemistry , vol.11 , pp. 541-547
    • Shrager, R.I.1    Sachs, D.H.2    Schechte, A.3    Cohen, J.S.4    Heller, S.R.5
  • 169
    • 84877875858 scopus 로고    scopus 로고
    • Unraveling a phosphorylation event in a folded protein by NMR spectroscopy: Phosphorylation of the Pin1 WW domain by PKA
    • Smet-Nocca C, Launay H, Wieruszeski JM, Lippens G, Landrieu I (2013) Unraveling a phosphorylation event in a folded protein by NMR spectroscopy: phosphorylation of the Pin1 WW domain by PKA. J Biomol NMR 55:323-337
    • (2013) J Biomol NMR , vol.55 , pp. 323-337
    • Smet-Nocca, C.1    Launay, H.2    Wieruszeski, J.M.3    Lippens, G.4    Landrieu, I.5
  • 170
    • 59349115177 scopus 로고    scopus 로고
    • Chemical mechanisms of histone lysine and arginine modifications
    • Smith BC, Denu JM (2009) Chemical mechanisms of histone lysine and arginine modifications. BBA-Gene Regul Mech 1789:45-57
    • (2009) BBA-Gene Regul Mech , vol.1789 , pp. 45-57
    • Smith, B.C.1    Denu, J.M.2
  • 172
    • 38048998514 scopus 로고    scopus 로고
    • Determination of electrostatic interaction energies and protonation state populations in enzyme active sites
    • Søndergaard CR, McIntosh LP, Pollastri G, Nielsen JE (2008) Determination of electrostatic interaction energies and protonation state populations in enzyme active sites. J Mol Biol 376:269-287
    • (2008) J Mol Biol , vol.376 , pp. 269-287
    • Søndergaard, C.R.1    McIntosh, L.P.2    Pollastri, G.3    Nielsen, J.E.4
  • 173
    • 0037452862 scopus 로고    scopus 로고
    • NMR determination of pKa values for Asp, Glu, His, and Lys mutants at each variable contiguous enzyme-inhibitor contact position of the turkey ovomucoid third domain
    • Song JK, Laskowski M, Qasim MA, Markley JL (2003) NMR determination of pKa values for Asp, Glu, His, and Lys mutants at each variable contiguous enzyme-inhibitor contact position of the turkey ovomucoid third domain. Biochemistry 42:2847-2856
    • (2003) Biochemistry , vol.42 , pp. 2847-2856
    • Song, J.K.1    Laskowski, M.2    Qasim, M.A.3    Markley, J.L.4
  • 174
    • 0034886835 scopus 로고    scopus 로고
    • Ionization properties of titratable groups in ribonuclease T1 - I. PKa values in the native state determined by two-dimensional heteronuclear NMR spectroscopy
    • Spitzner N, Löhr F, Pfeiffer S, Koumanov A, Karshikoff A, Rüterjans H (2001) Ionization properties of titratable groups in ribonuclease T1 - I. pKa values in the native state determined by two-dimensional heteronuclear NMR spectroscopy. Eur Biophys J with s 30:186-197
    • (2001) Eur Biophys J with S , vol.30 , pp. 186-197
    • Spitzner, N.1    Löhr, F.2    Pfeiffer, S.3    Koumanov, A.4    Karshikoff, A.5    Rüterjans, H.6
  • 177
  • 179
    • 4444260564 scopus 로고    scopus 로고
    • Determination of microscopic acid-base parameters from NMR pH titrations
    • Szakacs Z, Kraszni M, Noszal B (2004) Determination of microscopic acid-base parameters from NMR pH titrations. Anal Bioanal Chem 378:1428-1448
    • (2004) Anal Bioanal Chem , vol.378 , pp. 1428-1448
    • Szakacs, Z.1    Kraszni, M.2    Noszal, B.3
  • 180
    • 44349125669 scopus 로고    scopus 로고
    • Direct evidence for deprotonation of a lysine side chain buried in the hydrophobic core of a protein
    • Takayama Y, Castaneda CA, Chimenti M, Garcia-Moreno B, Iwahara J (2008a) Direct evidence for deprotonation of a lysine side chain buried in the hydrophobic core of a protein. J Am Chem Soc 130:6714-6715
    • (2008) J Am Chem Soc , vol.130 , pp. 6714-6715
    • Takayama, Y.1    Castaneda, C.A.2    Chimenti, M.3    Garcia-Moreno, B.4    Iwahara, J.5
  • 181
    • 52949107554 scopus 로고    scopus 로고
    • + groups with two-dimensional heteronuclear correlation spectroscopy
    • 2008JMagR.194.313T
    • + groups with two-dimensional heteronuclear correlation spectroscopy. J Magn Reson 194:313-316
    • (2008) J Magn Reson , vol.194 , pp. 313-316
    • Takayama, Y.1    Sahu, D.2    Iwahara, J.3
  • 184
    • 84896985217 scopus 로고    scopus 로고
    • Use of H/D isotope effects to gather information about hydrogen bonding and hydrogen exchange rates
    • 2014JMagR.241.148T
    • Takeda M, Miyanoiri Y, Terauchi T, Yang C-J, Kainosho M (2014) Use of H/D isotope effects to gather information about hydrogen bonding and hydrogen exchange rates. J Magn Reson 241:148-154
    • (2014) J Magn Reson , vol.241 , pp. 148-154
    • Takeda, M.1    Miyanoiri, Y.2    Terauchi, T.3    Yang, C.-J.4    Kainosho, M.5
  • 185
    • 78650615363 scopus 로고    scopus 로고
    • Sequence-specific random coil chemical shifts of intrinsically disordered proteins
    • Tamiola K, Acar B, Mulder FAA (2010) Sequence-specific random coil chemical shifts of intrinsically disordered proteins. J Am Chem Soc 132:18000-18003
    • (2010) J Am Chem Soc , vol.132 , pp. 18000-18003
    • Tamiola, K.1    Acar, B.2    Mulder, F.A.A.3
  • 186
    • 0021103512 scopus 로고
    • 1H-NMR study on the tautomerism of the imidazole ring of histidine-residues 1. Microscopic pK values and molar ratios of tautomers in histidine-containing peptides
    • 1H-NMR study on the tautomerism of the imidazole ring of histidine-residues 1. Microscopic pK values and molar ratios of tautomers in histidine-containing peptides. Biochim Biophys Acta 742:576-585
    • (1983) Biochim Biophys Acta , vol.742 , pp. 576-585
    • Tanokura, M.1
  • 187
    • 0027928701 scopus 로고
    • 13C chemical shifts of amino acids in aqueous-solution containing organic-solvents - Application to the secondary structure characterization of peptides in aqueous trifluoroethanol solution
    • 13C chemical shifts of amino acids in aqueous-solution containing organic-solvents - application to the secondary structure characterization of peptides in aqueous trifluoroethanol solution. J Biomol NMR 4:47-59
    • (1994) J Biomol NMR , vol.4 , pp. 47-59
    • Thanabal, V.1    Omecinsky, D.O.2    Reily, M.D.3    Cody, W.L.4
  • 188
    • 84868200531 scopus 로고    scopus 로고
    • Cell signaling, post-translational protein modifications and NMR spectroscopy
    • Theillet FX et al (2012) Cell signaling, post-translational protein modifications and NMR spectroscopy. J Biomol NMR 54:217-236
    • (2012) J Biomol NMR , vol.54 , pp. 217-236
    • Theillet, F.X.1
  • 189
    • 29244464347 scopus 로고    scopus 로고
    • The active site cysteine of ubiquitin-conjugating enzymes has a significantly elevated pKa: Functional implications
    • Tolbert BS, Tajc SG, Webb H, Snyder J, Nielsen JE, Miller BL, Basavappa R (2005) The active site cysteine of ubiquitin-conjugating enzymes has a significantly elevated pKa: functional implications. Biochemistry 44:16385-16391
    • (2005) Biochemistry , vol.44 , pp. 16385-16391
    • Tolbert, B.S.1    Tajc, S.G.2    Webb, H.3    Snyder, J.4    Nielsen, J.E.5    Miller, B.L.6    Basavappa, R.7
  • 190
    • 2342537653 scopus 로고    scopus 로고
    • Characterization of fluxional hydrogen-bonded complexes of acetic acid and acetate by NMR: Geometries and isotope and solvent effects
    • Tolstoy PM, Schah-Mohammedi P, Smirnov SN, Golubev NS, Denisov GS, Limbach HH (2004) Characterization of fluxional hydrogen-bonded complexes of acetic acid and acetate by NMR: geometries and isotope and solvent effects. J Am Chem Soc 126:5621-5634
    • (2004) J Am Chem Soc , vol.126 , pp. 5621-5634
    • Tolstoy, P.M.1    Schah-Mohammedi, P.2    Smirnov, S.N.3    Golubev, N.S.4    Denisov, G.S.5    Limbach, H.H.6
  • 191
    • 67949103448 scopus 로고    scopus 로고
    • Characterization of salt bridges to lysines in the protein G B1 domain
    • Tomlinson JH, Ullah S, Hansen PE, Williamson MP (2009) Characterization of salt bridges to lysines in the protein G B1 domain. J Am Chem Soc 131:4674-4684
    • (2009) J Am Chem Soc , vol.131 , pp. 4674-4684
    • Tomlinson, J.H.1    Ullah, S.2    Hansen, P.E.3    Williamson, M.P.4
  • 193
    • 85027924667 scopus 로고    scopus 로고
    • Indirect use of deuterium in solution NMR studies of protein structure and hydrogen bonding
    • Tugarinov V (2014) Indirect use of deuterium in solution NMR studies of protein structure and hydrogen bonding. Prog Nucl Magn Reson Spect 77:49-68
    • (2014) Prog Nucl Magn Reson Spect , vol.77 , pp. 49-68
    • Tugarinov, V.1
  • 194
    • 79953048897 scopus 로고    scopus 로고
    • Ab initio calculations of deuterium isotope effects on chemical shifts of salt-bridged lysines
    • Ullah S, Ishimoto T, Williamson MP, Hansen PE (2011) Ab initio calculations of deuterium isotope effects on chemical shifts of salt-bridged lysines. J Phys Chem B 115:3208-3215
    • (2011) J Phys Chem B , vol.115 , pp. 3208-3215
    • Ullah, S.1    Ishimoto, T.2    Williamson, M.P.3    Hansen, P.E.4
  • 195
    • 0037421933 scopus 로고    scopus 로고
    • Relations between protonation constants and titration curves in polyprotic acids: A critical view
    • Ullmann GM (2003) Relations between protonation constants and titration curves in polyprotic acids: a critical view. J Phys Chem B 107:1263-1271
    • (2003) J Phys Chem B , vol.107 , pp. 1263-1271
    • Ullmann, G.M.1
  • 196
    • 38549138986 scopus 로고    scopus 로고
    • BioMagResBank
    • Ulrich EL et al (2008) BioMagResBank. Nucleic Acids Res 36:D402-D408
    • (2008) Nucleic Acids Res , vol.36 , pp. 402-D408
    • Ulrich, E.L.1
  • 198
    • 84879529913 scopus 로고    scopus 로고
    • Measurement of active site ionization equilibria in the 670 kDa proteasome core particle using methyl-TROSY NMR
    • Velyvis A, Kay LE (2013) Measurement of active site ionization equilibria in the 670 kDa proteasome core particle using methyl-TROSY NMR. J Am Chem Soc 135:9259-9262
    • (2013) J Am Chem Soc , vol.135 , pp. 9259-9262
    • Velyvis, A.1    Kay, L.E.2
  • 199
    • 0028670214 scopus 로고
    • 15N resonance assignments and secondary structure-analysis of the hu protein from bacillus-stearothermophilus using 2-dimensional and 3-dimensional double-resonance and triple-resonance heteronuclear magnetic-resonance spectroscopy
    • 15N resonance assignments and secondary structure-analysis of the hu protein from bacillus-stearothermophilus using 2-dimensional and 3-dimensional double-resonance and triple-resonance heteronuclear magnetic-resonance spectroscopy. Biochemistry 33:14858-14870
    • (1994) Biochemistry , vol.33 , pp. 14858-14870
    • Vis, H.1    Boelens, R.2    Mariani, M.3    Stroop, R.4    Vorgias, C.E.5    Wilson, K.S.6    Kaptein, R.7
  • 200
    • 34347405094 scopus 로고    scopus 로고
    • NMR structure determination of a synthetic analogue of bacillomycin Lc reveals the strategic role of L-Asn1 in the natural iturinic antibiotics
    • 2007AcSpA.67.1374V
    • Volpon L et al (2007) NMR structure determination of a synthetic analogue of bacillomycin Lc reveals the strategic role of L-Asn1 in the natural iturinic antibiotics. Spectrochim Acta Part A 67:1374-1381
    • (2007) Spectrochim Acta Part A , vol.67 , pp. 1374-1381
    • Volpon, L.1
  • 202
    • 0037184476 scopus 로고    scopus 로고
    • Investigation of the neighboring residue effects on protein chemical shifts
    • Wang YJ, Jardetzky O (2002) Investigation of the neighboring residue effects on protein chemical shifts. J Am Chem Soc 124:14075-14084
    • (2002) J Am Chem Soc , vol.124 , pp. 14075-14084
    • Wang, Y.J.1    Jardetzky, O.2
  • 203
    • 0029757151 scopus 로고    scopus 로고
    • Solution NMR evidence that the HIV-1 protease catalytic aspartyl groups have different ionization states in the complex formed with the asymmetric drug KNI-272
    • Wang YX et al (1996) Solution NMR evidence that the HIV-1 protease catalytic aspartyl groups have different ionization states in the complex formed with the asymmetric drug KNI-272. Biochemistry 35:9945-9950
    • (1996) Biochemistry , vol.35 , pp. 9945-9950
    • Wang, Y.X.1
  • 204
    • 0038470479 scopus 로고
    • Deuterium-isotope effects on nuclear shielding constants and spin spin coupling-constants in the ammonium ion, ammonia, and water
    • Wasylishen RE, Friedrich JO (1987) Deuterium-isotope effects on nuclear shielding constants and spin spin coupling-constants in the ammonium ion, ammonia, and water. Can J Chem 65:2238-2243
    • (1987) Can J Chem , vol.65 , pp. 2238-2243
    • Wasylishen, R.E.1    Friedrich, J.O.2
  • 205
    • 0016594740 scopus 로고
    • 13C, H coupling-constants in imidazole and L-histidine
    • 13C, H coupling-constants in imidazole and L-histidine. Biochem J 147:605-607
    • (1975) Biochem J , vol.147 , pp. 605-607
    • Wasylishen, R.E.1    Tomlinson, G.2
  • 206
    • 0017387497 scopus 로고
    • 13C, H nuclear spin-spin coupling-constants in study of imidazole tautomerism in L-histidine, histamine, and related compounds
    • 13C, H nuclear spin-spin coupling-constants in study of imidazole tautomerism in L-histidine, histamine, and related compounds. Can J Biochem Cell B 55:579-582
    • (1977) Can J Biochem Cell B , vol.55 , pp. 579-582
    • Wasylishen, R.E.1    Tomlinson, G.2
  • 209
    • 0029116114 scopus 로고
    • Aspartic-acid 26 in reduced escherichia-coli thioredoxin has a pK(a) >9
    • Wilson NA, Barbar E, Fuchs JA, Woodward C (1995) Aspartic-acid 26 in reduced escherichia-coli thioredoxin has a pK(a) >9. Biochemistry 34:8931-8939
    • (1995) Biochemistry , vol.34 , pp. 8931-8939
    • Wilson, N.A.1    Barbar, E.2    Fuchs, J.A.3    Woodward, C.4
  • 210
    • 79451469120 scopus 로고    scopus 로고
    • Interpreting protein chemical shift data
    • Wishart DS (2011) Interpreting protein chemical shift data. Prog Nucl Magn Reson Spectr 58:62-87
    • (2011) Prog Nucl Magn Reson Spectr , vol.58 , pp. 62-87
    • Wishart, D.S.1
  • 211
    • 0029181728 scopus 로고
    • 15N random coil NMR chemical-shifts of the common amino-acids 1. Investigations of nearest-neighbor effects
    • 15N random coil NMR chemical-shifts of the common amino-acids 1. Investigations of nearest-neighbor effects. J Biomol NMR 5:67-81
    • (1995) J Biomol NMR , vol.5 , pp. 67-81
    • Wishart, D.S.1    Bigam, C.G.2    Holm, A.3    Hodges, R.S.4    Sykes, B.D.5
  • 212
    • 0000387893 scopus 로고
    • Nitrogen-14 nuclear magnetic resonance of azoles and their benzo derivatives
    • Witanowski M, Webb GA, Stefania L, Januszew H, Grabowsk Z (1972) Nitrogen-14 nuclear magnetic resonance of azoles and their benzo derivatives. Tetrahedron 28:637-653
    • (1972) Tetrahedron , vol.28 , pp. 637-653
    • Witanowski, M.1    Webb, G.A.2    Stefania, L.3    Januszew, H.4    Grabowsk, Z.5
  • 214
    • 0009708474 scopus 로고
    • Selective correlations of amide groups to glycine alpha-protons in proteins
    • Wittekind M, Metzler WJ, Mueller L (1993) Selective correlations of amide groups to glycine alpha-protons in proteins. J Magn Reson Ser B 101:214-217
    • (1993) J Magn Reson ser B , vol.101 , pp. 214-217
    • Wittekind, M.1    Metzler, W.J.2    Mueller, L.3
  • 215
    • 2642683990 scopus 로고
    • 1H-NMR spectrum of a protein by one-dimensional and two-dimensional NOE experiments
    • 1984JMagR.59.524W
    • 1H-NMR spectrum of a protein by one-dimensional and two-dimensional NOE experiments. J Magn Reson 59:524-529
    • (1984) J Magn Reson , vol.59 , pp. 524-529
    • Wu, X.J.1    Westler, W.M.2    Markley, J.L.3
  • 216
    • 0018782084 scopus 로고
    • Nuclear magnetic-resonance of labile protons in the basic pancreatic trypsin-inhibitor
    • Wüthrich K, Wagner G (1979) Nuclear magnetic-resonance of labile protons in the basic pancreatic trypsin-inhibitor. J Mol Biol 130:1-18
    • (1979) J Mol Biol , vol.130 , pp. 1-18
    • Wüthrich, K.1    Wagner, G.2
  • 217
    • 25444491291 scopus 로고    scopus 로고
    • 15N NMR spectra of guanidino groups in nonpolar environments
    • 15N NMR spectra of guanidino groups in nonpolar environments. J Phys Chem B 109:16953-16958
    • (2005) J Phys Chem B , vol.109 , pp. 16953-16958
    • Xiao, Y.W.1    Braiman, M.2
  • 219
    • 0027310404 scopus 로고
    • Complete assignments of magnetic resonances of ribonuclease-H from Escherichia coli by double-resonance and triple-resonance 2D and 3D NMR spectroscopies
    • Yamazaki T, Yoshida M, Nagayama K (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
    • (1993) Biochemistry , vol.32 , pp. 5656-5669
    • Yamazaki, T.1    Yoshida, M.2    Nagayama, K.3
  • 220
    • 0028114966 scopus 로고
    • NMR and X-ray evidence that the HIV protease catalytic aspartyl groups are protonated in the complex formed by the protease and a nonpeptide cyclic urea-based inhibitor
    • Yamazaki T et al (1994) NMR and X-ray evidence that the HIV protease catalytic aspartyl groups are protonated in the complex formed by the protease and a nonpeptide cyclic urea-based inhibitor. J Am Chem Soc 116:10791-10792
    • (1994) J Am Chem Soc , vol.116 , pp. 10791-10792
    • Yamazaki, T.1
  • 223
    • 0028170657 scopus 로고
    • PH titration of the histidine-residues of cyclophilin and FK506 binding-protein in the absence and presence of immunosuppressant ligands
    • Yu LP, Fesik SW (1994) pH titration of the histidine-residues of cyclophilin and FK506 binding-protein in the absence and presence of immunosuppressant ligands. Bioc Biophys Acta Prot Struct Molr Enzym 1209:24-32
    • (1994) Bioc Biophys Acta Prot Struct Molr Enzym , vol.1209 , pp. 24-32
    • Yu, L.P.1    Fesik, S.W.2
  • 225
    • 84896701049 scopus 로고    scopus 로고
    • NMR Studies on the dynamics of hydrogen bonds and ion pairs involving lysine side chains of proteins
    • Zandarashvili L, Esadze A, Iwahara J (2013) NMR Studies on the dynamics of hydrogen bonds and ion pairs involving lysine side chains of proteins. Adv Protein Chem Str 93:37-80
    • (2013) Adv Protein Chem Str , vol.93 , pp. 37-80
    • Zandarashvili, L.1    Esadze, A.2    Iwahara, J.3


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