메뉴 건너뛰기




Volumn 180, Issue 2, 2006, Pages 197-202

High-field (275 GHz) spin-label EPR for high-resolution polarity determination in proteins

Author keywords

High field EPR; Protein polarity; Protein proticity; Protein surface properties; Spin label EPR

Indexed keywords

AMINO ACIDS; HYDROGEN BONDS; MUTAGENESIS; OPTICAL RESOLVING POWER; PARAMETER ESTIMATION; PROTEINS; SURFACE PHENOMENA;

EID: 33646371707     PISSN: 10907807     EISSN: 10960856     Source Type: Journal    
DOI: 10.1016/j.jmr.2006.02.011     Document Type: Article
Times cited : (16)

References (12)
  • 1
    • 0034639884 scopus 로고    scopus 로고
    • High-field EPR studies of the structure and conformational changes of site-directed spin labeled bacteriorhodopsin
    • Steinhoff H.J., Savitsky A., Wegener C., Pfeiffer M., Plato M., and Möbius K. High-field EPR studies of the structure and conformational changes of site-directed spin labeled bacteriorhodopsin. Biochim. Biophys. Acta-Bioenerg. 1457 (2000) 253-262
    • (2000) Biochim. Biophys. Acta-Bioenerg. , vol.1457 , pp. 253-262
    • Steinhoff, H.J.1    Savitsky, A.2    Wegener, C.3    Pfeiffer, M.4    Plato, M.5    Möbius, K.6
  • 2
    • 0035892170 scopus 로고    scopus 로고
    • A multifrequency ESR study of the complex dynamics of membranes
    • Lou Y., Ge M.T., and Freed J.R. A multifrequency ESR study of the complex dynamics of membranes. J. Phys. Chem. B 105 (2001) 11053-11056
    • (2001) J. Phys. Chem. B , vol.105 , pp. 11053-11056
    • Lou, Y.1    Ge, M.T.2    Freed, J.R.3
  • 3
    • 0025346254 scopus 로고
    • Transmembrane protein-structure-spin labeling of Bacteriorhodopsin mutants
    • Altenbach C., Marti T., Khorana H.G., and Hubbell W.L. Transmembrane protein-structure-spin labeling of Bacteriorhodopsin mutants. Science 248 (1990) 1088-1092
    • (1990) Science , vol.248 , pp. 1088-1092
    • Altenbach, C.1    Marti, T.2    Khorana, H.G.3    Hubbell, W.L.4
  • 4
    • 0348222027 scopus 로고    scopus 로고
    • A continuous-wave and pulsed electron spin resonance spectrometer operating at 275 GHz
    • Blok H., Disselhorst J.A.J.M., Orlinskii S.B., and Schmidt J. A continuous-wave and pulsed electron spin resonance spectrometer operating at 275 GHz. J. Magn. Reson. 166 (2004) 92-99
    • (2004) J. Magn. Reson. , vol.166 , pp. 92-99
    • Blok, H.1    Disselhorst, J.A.J.M.2    Orlinskii, S.B.3    Schmidt, J.4
  • 5
    • 0035857235 scopus 로고    scopus 로고
    • Influence of solvent polarity and hydrogen bonding on the EPR parameters of a nitroxide spin label studied by 9-GHz and 95-GHz EPR spectroscopy and DFT calculations
    • Owenius R., Engström M., Lindgren M., and Huber M. Influence of solvent polarity and hydrogen bonding on the EPR parameters of a nitroxide spin label studied by 9-GHz and 95-GHz EPR spectroscopy and DFT calculations. J. Phys. Chem. A 105 (2001) 10967-10977
    • (2001) J. Phys. Chem. A , vol.105 , pp. 10967-10977
    • Owenius, R.1    Engström, M.2    Lindgren, M.3    Huber, M.4
  • 6
    • 0025953438 scopus 로고
    • Crystal-structure analysis of oxidized Pseudomonas aeruginosa azurin at pH 5.5 and pH 9.0-a pH-induced conformational transition involves a peptide-bond flip
    • Nar H., Messerschmidt A., Huber R., van de Kamp M., and Canters G.W. Crystal-structure analysis of oxidized Pseudomonas aeruginosa azurin at pH 5.5 and pH 9.0-a pH-induced conformational transition involves a peptide-bond flip. J. Mol. Biol. 221 (1991) 765-772
    • (1991) J. Mol. Biol. , vol.221 , pp. 765-772
    • Nar, H.1    Messerschmidt, A.2    Huber, R.3    van de Kamp, M.4    Canters, G.W.5
  • 7
    • 0037187560 scopus 로고    scopus 로고
    • Anti-cooperativity in the two electron oxidation of the S118C disulfide dimer of azurin
    • van Amsterdam I.M.C., Ubbink M., and Canters G.W. Anti-cooperativity in the two electron oxidation of the S118C disulfide dimer of azurin. Inorg. Chim. Acta 331 (2002) 296-302
    • (2002) Inorg. Chim. Acta , vol.331 , pp. 296-302
    • van Amsterdam, I.M.C.1    Ubbink, M.2    Canters, G.W.3
  • 8
    • 0345377701 scopus 로고    scopus 로고
    • Anisotropic spin label mobilities in azurin from 95 GHz electron paramagnetic resonance spectroscopy
    • Finiguerra M.G., van Amsterdam I.M.C., Alagaratnam S., Ubbink M., and Huber M. Anisotropic spin label mobilities in azurin from 95 GHz electron paramagnetic resonance spectroscopy. Chem. Phys. Lett. 382 (2003) 528-533
    • (2003) Chem. Phys. Lett. , vol.382 , pp. 528-533
    • Finiguerra, M.G.1    van Amsterdam, I.M.C.2    Alagaratnam, S.3    Ubbink, M.4    Huber, M.5
  • 9
    • 0037059138 scopus 로고    scopus 로고
    • Molecular orbital study of polarity and hydrogen bonding effects on the g and hyperfine tensors of site directed NO spin labelled bacteriorhodopsin
    • Plato M., Steinhoff H.J., Wegener C., Törring J.T., Savitsky A., and Möbius K. Molecular orbital study of polarity and hydrogen bonding effects on the g and hyperfine tensors of site directed NO spin labelled bacteriorhodopsin. Mol. Phys. 100 (2002) 3711-3721
    • (2002) Mol. Phys. , vol.100 , pp. 3711-3721
    • Plato, M.1    Steinhoff, H.J.2    Wegener, C.3    Törring, J.T.4    Savitsky, A.5    Möbius, K.6
  • 10
    • 84962425361 scopus 로고    scopus 로고
    • Density functional theory calculations of electron paramagnetic resonance parameters of a nitroxide spin label in tissue factor and factor VIIa protein complex
    • Engström M., Vaara J., Schimmelpfennig B., and Ågren H. Density functional theory calculations of electron paramagnetic resonance parameters of a nitroxide spin label in tissue factor and factor VIIa protein complex. J. Phys. Chem. B 106 (2002) 12354-12360
    • (2002) J. Phys. Chem. B , vol.106 , pp. 12354-12360
    • Engström, M.1    Vaara, J.2    Schimmelpfennig, B.3    Ågren, H.4
  • 11
    • 0039171268 scopus 로고    scopus 로고
    • Crystal structures of spin labeled T4 lysozyme mutants: implications for the interpretation of EPR spectra in terms of structure
    • Langen R., Oh K.J., Cascio D., and Hubbell W.L. Crystal structures of spin labeled T4 lysozyme mutants: implications for the interpretation of EPR spectra in terms of structure. Biochemistry 39 (2000) 8396-8405
    • (2000) Biochemistry , vol.39 , pp. 8396-8405
    • Langen, R.1    Oh, K.J.2    Cascio, D.3    Hubbell, W.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.