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Volumn 1764, Issue 5, 2006, Pages 856-862

NMR studies of BPTI aggregation by using paramagnetic relaxation reagents

Author keywords

BPTI; Gd(III)DTPA BMA; NMR; Paramagnetic probe; Protein aggregation; Surface accessibility; TEMPOL

Indexed keywords

APROTININ; GADOVERSETAMIDE; PROTON; REAGENT; TEMPOL;

EID: 33646507488     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2006.02.013     Document Type: Article
Times cited : (16)

References (24)
  • 1
    • 0029868304 scopus 로고    scopus 로고
    • Locating and characterizing binding sites on proteins
    • Mattos C., and Ringe D. Locating and characterizing binding sites on proteins. Nat. Biotechnol. 14 (1996) 595-599
    • (1996) Nat. Biotechnol. , vol.14 , pp. 595-599
    • Mattos, C.1    Ringe, D.2
  • 2
    • 0029584688 scopus 로고
    • What makes a binding site a binding site
    • Ringe D. What makes a binding site a binding site. Curr. Opin. Struct. Biol. 5 (1995) 825-829
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 825-829
    • Ringe, D.1
  • 4
    • 0030965629 scopus 로고    scopus 로고
    • Organic solvents identify specific ligand binding sites on protein surfaces
    • Liepinsh E., and Otting G. Organic solvents identify specific ligand binding sites on protein surfaces. Nat. Biotechnol. 15 (1997) 264-268
    • (1997) Nat. Biotechnol. , vol.15 , pp. 264-268
    • Liepinsh, E.1    Otting, G.2
  • 9
    • 0037160426 scopus 로고    scopus 로고
    • Identification of protein surfaces by NMR measurements with a pramagnetic Gd(III) chelate
    • Pintacuda G., and Otting G. Identification of protein surfaces by NMR measurements with a pramagnetic Gd(III) chelate. J. Am. Chem. Soc. 124 (2002) 372-373
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 372-373
    • Pintacuda, G.1    Otting, G.2
  • 10
    • 0034737315 scopus 로고    scopus 로고
    • The BPTI decamer observed in acidic pH crystal forms pre-exists as a stable species in solution
    • Hamiaux C., Perez J., Prange T., Veesler S., Ries-Kautt M., and Vachette P. The BPTI decamer observed in acidic pH crystal forms pre-exists as a stable species in solution. J. Mol. Biol. 297 (2000) 697-712
    • (2000) J. Mol. Biol. , vol.297 , pp. 697-712
    • Hamiaux, C.1    Perez, J.2    Prange, T.3    Veesler, S.4    Ries-Kautt, M.5    Vachette, P.6
  • 11
    • 0026417273 scopus 로고
    • Self-association of bovine pancreatic trypsin inhibitor: specific or nonspecific
    • Zielenkiewicz P., Georgalis Y., and Saenger W. Self-association of bovine pancreatic trypsin inhibitor: specific or nonspecific. Biopolymers 31 (1991) 1347-1349
    • (1991) Biopolymers , vol.31 , pp. 1347-1349
    • Zielenkiewicz, P.1    Georgalis, Y.2    Saenger, W.3
  • 12
    • 0030893784 scopus 로고    scopus 로고
    • A pulsed-field gradient NMR study of bovine pancreatic trypsin inhibitor self-association
    • Ilyina E., Roongta V., Pan H., Woodward C., and Mayo K.H. A pulsed-field gradient NMR study of bovine pancreatic trypsin inhibitor self-association. Biochemistry 36 (1997) 3383-3388
    • (1997) Biochemistry , vol.36 , pp. 3383-3388
    • Ilyina, E.1    Roongta, V.2    Pan, H.3    Woodward, C.4    Mayo, K.H.5
  • 13
    • 0038693409 scopus 로고    scopus 로고
    • Protein self-association in solution: the bovine pancreatic trypsin inhibitor decamer
    • Gottschalk M., Venu K., and Halle B. Protein self-association in solution: the bovine pancreatic trypsin inhibitor decamer. Biophys. J. 84 (2003) 3941-3958
    • (2003) Biophys. J. , vol.84 , pp. 3941-3958
    • Gottschalk, M.1    Venu, K.2    Halle, B.3
  • 14
    • 0023660041 scopus 로고
    • Hydrogen exchange kinetics of surface peptide amides in bovine pancreatic trypsin inhibitor
    • Tuchsen E., and Woodward C. Hydrogen exchange kinetics of surface peptide amides in bovine pancreatic trypsin inhibitor. J. Mol. Biol. 193 (1987) 793-802
    • (1987) J. Mol. Biol. , vol.193 , pp. 793-802
    • Tuchsen, E.1    Woodward, C.2
  • 15
    • 0026795399 scopus 로고
    • Determination of a high-quality nuclear magnetic resonance solution structure of the bovine pancreatic trypsin inhibitor and comparison with three crystal structures
    • Berndt K.D., Guntert P., Orbons L.P., and Wuthrich K. Determination of a high-quality nuclear magnetic resonance solution structure of the bovine pancreatic trypsin inhibitor and comparison with three crystal structures. J. Mol. Biol. 227 (1992) 757-775
    • (1992) J. Mol. Biol. , vol.227 , pp. 757-775
    • Berndt, K.D.1    Guntert, P.2    Orbons, L.P.3    Wuthrich, K.4
  • 16
    • 79960698472 scopus 로고
    • Water suppression that works. Excitation sculpting using arbitrary wave-forms and pulsed-field gradients
    • Hwang T.L., and Shaka A.J. Water suppression that works. Excitation sculpting using arbitrary wave-forms and pulsed-field gradients. J. Magn. Reson., A 112 (1995) 275-279
    • (1995) J. Magn. Reson., A , vol.112 , pp. 275-279
    • Hwang, T.L.1    Shaka, A.J.2
  • 17
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: a program for display and analysis of macromolecular structure
    • Koradi R., Billeter M., and Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structure. J. Mol. Graph. 14 (1996) 51-55
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 20
    • 0026663387 scopus 로고
    • Dynamics of methyl groups in proteins as studied by proton-detected 13C NMR spectroscopy. Application to the leucine residues of staphylococcal nuclease
    • Nicholson L.K., Kay L.E., Baldisseri D.M., Arango J., Young P.E., Bax A., and Torchia D.A. Dynamics of methyl groups in proteins as studied by proton-detected 13C NMR spectroscopy. Application to the leucine residues of staphylococcal nuclease. Biochemistry 31 (1992) 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
  • 21
    • 0002228715 scopus 로고    scopus 로고
    • NMR of paramagnetic substances
    • Bertini I., and Luchinat C. NMR of paramagnetic substances. Coord. Chem. Rev. 150 (1996) 1-300
    • (1996) Coord. Chem. Rev. , vol.150 , pp. 1-300
    • Bertini, I.1    Luchinat, C.2
  • 22
    • 0019994988 scopus 로고
    • The stereochemistry and dynamics of natural products and biopolymers from proton relaxation spectroscopy: spin-label delineation of inner and outer protons of gramicidin S including hydrogen bonds
    • Niccolai N., Valensin G., Rossi C., and Gibbons W.A. The stereochemistry and dynamics of natural products and biopolymers from proton relaxation spectroscopy: spin-label delineation of inner and outer protons of gramicidin S including hydrogen bonds. J. Am. Chem. Soc. 104 (1982) 1534-1537
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 1534-1537
    • Niccolai, N.1    Valensin, G.2    Rossi, C.3    Gibbons, W.A.4
  • 23
    • 37049094134 scopus 로고
    • Confirmation of the solution structure of tyrocidine a using perturbation of proton relaxation rates by nitroxide spin labels
    • Zhou N., Mascagni P., Gibbons W.A., Niccolai N., Rossi C., and Wyssbrod H. Confirmation of the solution structure of tyrocidine a using perturbation of proton relaxation rates by nitroxide spin labels. J. Chem. Soc., Perkin II (1985) 581-587
    • (1985) J. Chem. Soc., Perkin II , pp. 581-587
    • Zhou, N.1    Mascagni, P.2    Gibbons, W.A.3    Niccolai, N.4    Rossi, C.5    Wyssbrod, H.6
  • 24
    • 0031014046 scopus 로고    scopus 로고
    • Kinetic analysis of macromolecular interactions using surface plasmon resonance biosensors
    • Myzka D.G. Kinetic analysis of macromolecular interactions using surface plasmon resonance biosensors. Curr. Opin. Biotechnol. 8 (1997) 50-57
    • (1997) Curr. Opin. Biotechnol. , vol.8 , pp. 50-57
    • Myzka, D.G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.