메뉴 건너뛰기




Volumn 38, Issue 3, 2007, Pages 199-212

Fractional 13C enrichment of isolated carbons using [1-13C]- or [2-13C]-glucose facilitates the accurate measurement of dynamics at backbone Cα and side-chain methyl positions in proteins

Author keywords

13C relaxation measurements; 1 13C glucose; 2 13C glucose; CPMG relaxation dispersion; Protein expression; Selective 13C labeling; T1

Indexed keywords

AMINO ACID; CARBON 13; GLUCOSE; ISOLEUCINE; PROTEIN; THREONINE; CARBON; DRUG DERIVATIVE; METHANE; METHYL RADICAL; UNCLASSIFIED DRUG;

EID: 34250903564     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-007-9158-6     Document Type: Article
Times cited : (159)

References (44)
  • 1
    • 33646557015 scopus 로고    scopus 로고
    • Functional dynamics of human FKBP12 revealed by methyl C-13 rotating frame relaxation dispersion NMR spectroscopy
    • Brath U, Akke M, Yang DW, Kay LE, Mulder FAA (2006) Functional dynamics of human FKBP12 revealed by methyl C-13 rotating frame relaxation dispersion NMR spectroscopy. J Am Chem Soc 128:5718-5727
    • (2006) J Am Chem Soc , vol.128 , pp. 5718-5727
    • Brath, U.1    Akke, M.2    Yang, D.W.3    Kay, L.E.4    Mulder, F.A.A.5
  • 2
    • 17144415881 scopus 로고    scopus 로고
    • An N-15 NMR spin relaxation dispersion study of the folding of a pair of engineered mutants of apocytochrome b(562)
    • Choy WY, Zhou Z, Bai YW, Kay LE (2005) An N-15 NMR spin relaxation dispersion study of the folding of a pair of engineered mutants of apocytochrome b(562). J Am Chem Soc 127:5066-5072
    • (2005) J Am Chem Soc , vol.127 , pp. 5066-5072
    • Choy, W.Y.1    Zhou, Z.2    Bai, Y.W.3    Kay, L.E.4
  • 3
    • 0036405903 scopus 로고    scopus 로고
    • Redesign of a four-helix bundle protein by phage display coupled with proteolysis and structural characterization by NMR and x-ray crystallography
    • Chu R, Takei J, Knowlton JR, Andrykovitch M, Pei WH, Kajava AV, Steinbach PJ, Ji XH, Bai YW (2002) Redesign of a four-helix bundle protein by phage display coupled with proteolysis and structural characterization by NMR and x-ray crystallography. J Mol Biol 323:253-262
    • (2002) J Mol Biol , vol.323 , pp. 253-262
    • Chu, R.1    Takei, J.2    Knowlton, J.R.3    Andrykovitch, M.4    Pei, W.H.5    Kajava, A.V.6    Steinbach, P.J.7    Ji, X.H.8    Bai, Y.W.9
  • 4
    • 0000244137 scopus 로고    scopus 로고
    • Measurement of C-13(alpha)-(CO)-C-13 cross-relaxation rates in N-15-(IC)-C-13-labeled proteins
    • Cordier F, Brutscher B, Marion D (1996) Measurement of C-13(alpha)-(CO)-C-13 cross-relaxation rates in N-15-(IC)-C-13-labeled proteins. J Biomol NMR 7:163-168
    • (1996) J Biomol NMR , vol.7 , pp. 163-168
    • Cordier, F.1    Brutscher, B.2    Marion, D.3
  • 6
    • 0023522384 scopus 로고
    • Two-dimensional H-1-NMR study of human ubiquitin: A main chain directed assignment and structure analysis
    • Di Stefano DL, Wand AJ (1987) Two-dimensional H-1-NMR study of human ubiquitin: A main chain directed assignment and structure analysis. Biochemistry 26:7272-7281
    • (1987) Biochemistry , vol.26 , pp. 7272-7281
    • Di Stefano, D.L.1    Wand, A.J.2
  • 7
    • 0034821018 scopus 로고    scopus 로고
    • Cross-correlated chemical shift modulation: A signature of slow internal motions in proteins
    • Fruh D, Tolman JR, Bodenhausen G, Zwahlen C (2001) Cross-correlated chemical shift modulation: A signature of slow internal motions in proteins. J Am Chem Soc 123:4810-4816
    • (2001) J Am Chem Soc , vol.123 , pp. 4810-4816
    • Fruh, D.1    Tolman, J.R.2    Bodenhausen, G.3    Zwahlen, C.4
  • 8
    • 44949280676 scopus 로고
    • Band-selective radiofrequency pulses
    • Geen H, Freeman R (1991) Band-selective radiofrequency pulses. J Magn Reson 93:93-141
    • (1991) J Magn Reson , vol.93 , pp. 93-141
    • Geen, H.1    Freeman, R.2
  • 9
    • 34250889932 scopus 로고    scopus 로고
    • SPARKY 3, University of California, San Francisco
    • Goddard TD and Kneller DG SPARKY 3, University of California, San Francisco
    • Goddard, T.D.1    Kneller, D.G.2
  • 10
    • 0345306309 scopus 로고    scopus 로고
    • Disulfide bond isomerization in basic pancreatic trypsin inhibitor: Multisite chemical exchange quantified by CPMG relaxation dispersion and chemical shift modeling
    • Grey MJ, Wang CY, Palmer AG, III (2003) Disulfide bond isomerization in basic pancreatic trypsin inhibitor: Multisite chemical exchange quantified by CPMG relaxation dispersion and chemical shift modeling. J Am Chem Soc 125:14324-14335
    • (2003) J Am Chem Soc , vol.125 , pp. 14324-14335
    • Grey, M.J.1    Wang, C.Y.2    Palmer III, A.G.3
  • 11
    • 1842503159 scopus 로고    scopus 로고
    • Carbonyl carbon transverse relaxation dispersion measurements and ms-mu s timescale motion in a protein hydrogen bond network
    • Ishima R, Baber J, Louis JM, Torchia DA (2004) Carbonyl carbon transverse relaxation dispersion measurements and ms-mu s timescale motion in a protein hydrogen bond network. J Biomol NMR 29:187-198
    • (2004) J Biomol NMR , vol.29 , pp. 187-198
    • Ishima, R.1    Baber, J.2    Louis, J.M.3    Torchia, D.A.4
  • 12
    • 0033572874 scopus 로고    scopus 로고
    • Transverse C-13 relaxation of CHD2 methyl isotopmers to detect slow conformational changes of protein side chains
    • Ishima R, Louis JM, Torchia DA (1999) Transverse C-13 relaxation of CHD2 methyl isotopmers to detect slow conformational changes of protein side chains. J Am Chem Soc 121:11589-11590
    • (1999) J Am Chem Soc , vol.121 , pp. 11589-11590
    • Ishima, R.1    Louis, J.M.2    Torchia, D.A.3
  • 13
    • 0034740288 scopus 로고    scopus 로고
    • Optimized labeling of (CHD2)-C-13 methyl isotopomers in perdeuterated proteins: Potential advantages for C-13 relaxation studies of methyl dynamics of larger proteins
    • Ishima R, Louis JM, Torchia DA (2001) Optimized labeling of (CHD2)-C-13 methyl isotopomers in perdeuterated proteins: Potential advantages for C-13 relaxation studies of methyl dynamics of larger proteins. J Biomol NMR 21:167-171
    • (2001) J Biomol NMR , vol.21 , pp. 167-171
    • Ishima, R.1    Louis, J.M.2    Torchia, D.A.3
  • 14
    • 20444409471 scopus 로고    scopus 로고
    • The structure of the major transition state for folding of an FF domain from experiment and simulation
    • Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR (2005) The structure of the major transition state for folding of an FF domain from experiment and simulation. J Mol Biol 350:363-378
    • (2005) J Mol Biol , vol.350 , pp. 363-378
    • Jemth, P.1    Day, R.2    Gianni, S.3    Khan, F.4    Allen, M.5    Daggett, V.6    Fersht, A.R.7
  • 15
    • 0024449503 scopus 로고
    • Backbone dynamics of proteins as studied by N-15 inverse detected heteronuclear NMR-spectroscopy - Application to Staphylococcal nuclease
    • Kay LE, Torchia DA, Bax A (1989) Backbone dynamics of proteins as studied by N-15 inverse detected heteronuclear NMR-spectroscopy - application to Staphylococcal nuclease. Biochemistry 28:8972-8979
    • (1989) Biochemistry , vol.28 , pp. 8972-8979
    • Kay, L.E.1    Torchia, D.A.2    Bax, A.3
  • 17
    • 0028434564 scopus 로고
    • Correlation between N-15 NMR chemical-shifts in proteins and secondary structure
    • Le HB, Oldfield E (1994) Correlation between N-15 NMR chemical-shifts in proteins and secondary structure. J Biomol NMR 4:341-348
    • (1994) J Biomol NMR , vol.4 , pp. 341-348
    • Le, H.B.1    Oldfield, E.2
  • 18
    • 0031154310 scopus 로고    scopus 로고
    • Improved labeling strategy for C-13 relaxation measurements of methyl groups in proteins
    • Lee AL, Urbauer JL, Wand AJ (1997) Improved labeling strategy for C-13 relaxation measurements of methyl groups in proteins. J Biomol NMR 9:437-440
    • (1997) J Biomol NMR , vol.9 , pp. 437-440
    • Lee, A.L.1    Urbauer, J.L.2    Wand, A.J.3
  • 19
    • 0029905210 scopus 로고    scopus 로고
    • Dynamical mapping of E. coli thioredoxin via C-13 NMR relaxation analysis
    • LeMaster DM, Kushlan DM (1996) Dynamical mapping of E. coli thioredoxin via C-13 NMR relaxation analysis. J Am Chem Soc 118:9255-9264
    • (1996) J Am Chem Soc , vol.118 , pp. 9255-9264
    • LeMaster, D.M.1    Kushlan, D.M.2
  • 20
    • 0033577288 scopus 로고    scopus 로고
    • A relaxation-compensated Carr-Purcell-Meiboom-Gill sequence for characterizing chemical exchange by NMR spectroscopy
    • Loria JP, Rance M, Palmer AG, III (1999) A relaxation-compensated Carr-Purcell-Meiboom-Gill sequence for characterizing chemical exchange by NMR spectroscopy. J Am Chem Soc 121:2331-2332
    • (1999) J Am Chem Soc , vol.121 , pp. 2331-2332
    • Loria, J.P.1    Rance, M.2    Palmer III, A.G.3
  • 21
  • 22
    • 0025726542 scopus 로고
    • Gene synthesis, expression in Escherichia Coli, purification and characterization of the recombinant bovine acyl-CoA-binding protein
    • Mandrup S, Hojrup P, Kristiansen K, Knudsen J (1991) Gene synthesis, expression in Escherichia Coli, purification and characterization of the recombinant bovine acyl-CoA-binding protein. Biochem J 276:817-823
    • (1991) Biochem J , vol.276 , pp. 817-823
    • Mandrup, S.1    Hojrup, P.2    Kristiansen, K.3    Knudsen, J.4
  • 23
    • 33645834303 scopus 로고    scopus 로고
    • New tools provide new insights in NMR studies of protein dynamics
    • Mittermaier A, Kay LE (2006) New tools provide new insights in NMR studies of protein dynamics. Science 312:224-228
    • (2006) Science , vol.312 , pp. 224-228
    • Mittermaier, A.1    Kay, L.E.2
  • 24
    • 0037138654 scopus 로고    scopus 로고
    • Slow internal dynamics in proteins: Application of NMR relaxation dispersion spectroscopy to methyl groups in a cavity mutant of T4 lysozyme
    • Mulder FAA, Hon B, Mittermaier A, Dahlquist FW, Kay LE (2002) Slow internal dynamics in proteins: Application of NMR relaxation dispersion spectroscopy to methyl groups in a cavity mutant of T4 lysozyme. J Am Chem Soc 124:1443-1451
    • (2002) J Am Chem Soc , vol.124 , pp. 1443-1451
    • Mulder, F.A.A.1    Hon, B.2    Mittermaier, A.3    Dahlquist, F.W.4    Kay, L.E.5
  • 26
    • 0026663387 scopus 로고
    • Dynamics of methyl-groups in proteins as studied by proton-detected C-13 NMR-spectroscopy - Application to the leucine residues of Staphylococcal nuclease
    • Nicholson LK, Kay LE, Baldisseri DM, Arango J, Young PE, Bax A, Torchia DA (1992) Dynamics of methyl-groups in proteins as studied by proton-detected C-13 NMR-spectroscopy - application to the leucine residues of Staphylococcal nuclease. Biochemistry 31:5253-5263
    • (1992) Biochemistry , vol.31 , pp. 5253-5263
    • Nicholson, L.K.1    Kay, L.E.2    Baldisseri, D.M.3    Arango, J.4    Young, P.E.5    Bax, A.6    Torchia, D.A.7
  • 27
    • 0034607977 scopus 로고    scopus 로고
    • Investigation of the TCA cycle and the glyoxylate shunt in Escherichia coli BL21 and JM109 using C-13-NMR/MS
    • Noronha SB, Yeh HJC, Spande TF, Shiloach J (2000) Investigation of the TCA cycle and the glyoxylate shunt in Escherichia coli BL21 and JM109 using C-13-NMR/MS. Biotechnol Bioeng 68:316-327
    • (2000) Biotechnol Bioeng , vol.68 , pp. 316-327
    • Noronha, S.B.1    Yeh, H.J.C.2    Spande, T.F.3    Shiloach, J.4
  • 28
    • 0030758958 scopus 로고    scopus 로고
    • An empirical correlation between amide deuterium isotope effects on C-13(alpha) chemical shifts and protein backbone conformation
    • Ottiger M, Bax A (1997) An empirical correlation between amide deuterium isotope effects on C-13(alpha) chemical shifts and protein backbone conformation. J Am Chem Soc 119:8070-8075
    • (1997) J Am Chem Soc , vol.119 , pp. 8070-8075
    • Ottiger, M.1    Bax, A.2
  • 29
    • 4243155782 scopus 로고    scopus 로고
    • NMR characterization of the dynamics of biomacromolecules
    • Palmer AG, III (2004) NMR characterization of the dynamics of biomacromolecules. Chem Rev 104:3623-3640
    • (2004) Chem Rev , vol.104 , pp. 3623-3640
    • Palmer III, A.G.1
  • 30
    • 0034919305 scopus 로고    scopus 로고
    • Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules
    • Palmer AG, III, Kroenke CD, Loria JP (2001) Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules. Method Enzymol 339:204-238
    • (2001) Method Enzymol , vol.339 , pp. 204-238
    • Palmer III, A.G.1    Kroenke, C.D.2    Loria, J.P.3
  • 31
    • 0028674384 scopus 로고
    • Investigation of Protein Motions Via Relaxation Measurements
    • Peng JW, Wagner G (1994) Investigation of Protein Motions Via Relaxation Measurements. Method Enzymol 239:563-596
    • (1994) Method Enzymol , vol.239 , pp. 563-596
    • Peng, J.W.1    Wagner, G.2
  • 33
    • 0034809982 scopus 로고    scopus 로고
    • Probing slow time scale dynamics at methyl-containing side chains in proteins by relaxation dispersion NMR measurements: Application to methionine residues in a cavity mutant of T4 lysozyme
    • Skrynnikov NR, Mulder FAA, Hon B, Dahlquist FW, Kay LE (2001) Probing slow time scale dynamics at methyl-containing side chains in proteins by relaxation dispersion NMR measurements: Application to methionine residues in a cavity mutant of T4 lysozyme. J Am Chem Soc 123:4556-4566
    • (2001) J Am Chem Soc , vol.123 , pp. 4556-4566
    • Skrynnikov, N.R.1    Mulder, F.A.A.2    Hon, B.3    Dahlquist, F.W.4    Kay, L.E.5
  • 34
    • 0347610773 scopus 로고
    • Empirical correlation between protein backbone conformation and C-alpha and C-beta C-13 nuclear magnetic resonance chemical shifts
    • Spera S, Bax A (1991) Empirical correlation between protein backbone conformation and C-alpha and C-beta C-13 nuclear magnetic resonance chemical shifts. J Am Chem Soc 113:5490-5492
    • (1991) J Am Chem Soc , vol.113 , pp. 5490-5492
    • Spera, S.1    Bax, A.2
  • 35
    • 33644644556 scopus 로고    scopus 로고
    • Biosynthetic C-13 labeling of aromatic side chains in proteins for NMR relaxation measurements
    • Teilum K, Brath U, Lundström P, Akke M (2006) Biosynthetic C-13 labeling of aromatic side chains in proteins for NMR relaxation measurements. J Am Chem Soc 128:2506-2507
    • (2006) J Am Chem Soc , vol.128 , pp. 2506-2507
    • Teilum, K.1    Brath, U.2    Lundström, P.3    Akke, M.4
  • 37
    • 0141954227 scopus 로고    scopus 로고
    • Molecular structure and dynamics of proteins in solution: Insights derived from high-resolution NMR approaches
    • Torchia DA, Ishima R (2003) Molecular structure and dynamics of proteins in solution: Insights derived from high-resolution NMR approaches. Pure App Chem 75:1371-1381
    • (2003) Pure App Chem , vol.75 , pp. 1371-1381
    • Torchia, D.A.1    Ishima, R.2
  • 38
  • 40
    • 0038037171 scopus 로고    scopus 로고
    • Temperature dependence of anisotropic protein backbone dynamics
    • Wang TZ, Cai S, Zuiderweg ERP (2003) Temperature dependence of anisotropic protein backbone dynamics. J Am Chem Soc 125:8639-8643
    • (2003) J Am Chem Soc , vol.125 , pp. 8639-8643
    • Wang, T.Z.1    Cai, S.2    Zuiderweg, E.R.P.3
  • 41
    • 0028393784 scopus 로고
    • The C-13 chemical-shift index-a simple method for the identification of protein secondary structure using C-13 chemical-shift data
    • Wishart DS, Sykes BD (1994) The C-13 chemical-shift index-a simple method for the identification of protein secondary structure using C-13 chemical-shift data. J Biomol NMR 4:171-180
    • (1994) J Biomol NMR , vol.4 , pp. 171-180
    • Wishart, D.S.1    Sykes, B.D.2
  • 42
    • 0037114648 scopus 로고    scopus 로고
    • Probing multiple effects on N-15, C-13 alpha, C-13 beta, and C-13 ' chemical shifts in peptides using density functional theory
    • Xu XP, Case DA (2002) Probing multiple effects on N-15, C-13 alpha, C-13 beta, and C-13 ' chemical shifts in peptides using density functional theory. Biopolymers 65:408-423
    • (2002) Biopolymers , vol.65 , pp. 408-423
    • Xu, X.P.1    Case, D.A.2
  • 43
    • 0000733545 scopus 로고
    • NMR experiments for the measurement of carbon relaxation properties in highly enriched, uniformly C-13, N-15-labeled proteins-Application to C-13(alpha) carbons
    • Yamazaki T, Muhandiram R, Kay LE (1994) NMR experiments for the measurement of carbon relaxation properties in highly enriched, uniformly C-13, N-15-labeled proteins-Application to C-13(alpha) carbons. J Am Chem Soc 116:8266-8278
    • (1994) J Am Chem Soc , vol.116 , pp. 8266-8278
    • Yamazaki, T.1    Muhandiram, R.2    Kay, L.E.3
  • 44
    • 0001066543 scopus 로고    scopus 로고
    • Study of protein dynamics in solution by measurement of C-13(alpha)-(CO)-C-13 NOE and (CO)-C-13 longitudinal relaxation
    • Zeng L, Fischer MWF, Zuiderweg ERP (1996) Study of protein dynamics in solution by measurement of C-13(alpha)-(CO)-C-13 NOE and (CO)-C-13 longitudinal relaxation. J Biomol NMR 7:157-162
    • (1996) J Biomol NMR , vol.7 , pp. 157-162
    • Zeng, L.1    Fischer, M.W.F.2    Zuiderweg, E.R.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.