Neutron inelastic scattering as a high-resolution vibrational spectroscopy: New tool for the study of protein dynamics

Spectroscopy

Volumn 17, Issue 2-3, 2003, Pages 529-535

  Kataoka, Mikio ^a   Kamikubo, Hironari ^a   Nakagawa, Hiroshi ^a   Parker, Stewart F ^b   Smith, Jeremy C ^c  

^a NARA INSTITUTE OF SCIENCE AND TECHNOLOGY   (Japan)

^b RUTHERFORD APPLETON LABORATORY   (United Kingdom)

^c UNIVERSITY OF HEIDELBERG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; COMPOSITION; PROTEINS; SPECTROSCOPIC ANALYSIS;

VIBRATIONAL SPECTROSCOPY;

NEUTRON SCATTERING;

BACTERIAL ENZYME; BACTERIAL PROTEIN; NUCLEASE;

CONFERENCE PAPER; ENERGY; ESCHERICHIA COLI; GENE OVEREXPRESSION; MOLECULAR DYNAMICS; NEUTRON SCATTERING; NONHUMAN; PROTEIN ANALYSIS; SPECTROSCOPY; STAPHYLOCOCCUS; TEMPERATURE; VIBRATION;

EID: 0038369237     PISSN: 07124813     EISSN: None     Source Type: Journal    
DOI: 10.1155/2003/907042     Document Type: Conference Paper

References (16)

1. J.C. Smith, Protein dynamics: Comparison of simulations with inelastic neutron scattering experiments, Quart. Rev. Biophys. 24 (1991), 227-291.
2. A.V. Goupil-Lamy, J.C. Smith, J. Yunoki, S.F. Parker and M. Kataoka, High-resolution vibrational inelastic neutron scattering: A new spectroscopic tool for globular proteins, J. Amer. Chem. Soc. 119 (1997), 9268-9273.
3. M. Kataoka, H. Kamikubo, J. Yunoki, F. Tokunaga, T. Kanaya, Y. Izumi and K. Shibata, Low energy dynamics of globular proteins studied by inelastic neutron scattering, J. Phys. Chem. Solid 60 (1999), 1285-1289.
4. J.M. Flanagan, M. Kataoka, D. Shortle and D. M. Engelman, Truncated staphylococcal nuclease is compact but disordered, Proc. Natl. Acad. Sci. USA 89 (1992), 748-752.
5. A. Lamy and J.C. Smith, Denaturation of truncated staphylococcal nuclease in molecular dynamics simulation at 300 K, J. Amer. Chem. Soc. 118 (1996), 7326-7328.
6. G. Rubinstenn, G.W. Vuister, F.A. Mulder, P.E. Dux, R. Boelens, K.J. Hellingwerf and R. Kaptein, Structural and dynamic changes of photoactive yellow protein during its photocycle in solution, Nature Struct. Biol. 5 (1998), 568-570.
7. S. Ohishi, N. Shimizu, K. Mihara, Y. Imamaoto and M. Kataoka, Light induces destabilization of photoactive yellow protein, Biochemistry 40 (2001), 2854-2859.
8. D. Shortle, Guanidine hydrochloride denaturation studies of mutant forms of staphylococcal nuclease, J. Cell. Biochem. 30 (1986), 281-289.
9. A.T. Alexandrescu, C. Abeygunawardana and D. Shortle, Structure and dynamics of a denatured 131-residue fragment of staphylococcal nuclease: A heteronuclear NMR study, Biochemistry 33 (1994), 1063-1072.
10. K. Mihara, O. Hisatomi, Y. Imamoto, M. Kataoka and F. Tokunaga, Functional expression and site-directed mutaganesis of photoactive yellow protein, J. Biochem. 121 (1997), 876-880.
11. S.F. Parker, C.J. Carlile, T. Pike, J. Tomkinson, R.J. Newport, C. Andreani, F.P. Ricci, F. Sachetti and M. Zoppi, TOSCA: A world class inelastic neutron spectrometer, Physica B 241-243 (1998), 154-156.
12. K. Kuroda, Protein internal motions studied by molecular dynamics and normal mode analysis, Master's thesis, Graduate School of Science, Kyoto University, 1998.
13. T. Nishikawa and N. Go, Normal modes of vibration in bovine pancreatic trypsin inhibitor and its mechanical property, Proteins: Struct. Funct. Genet. 2 (1987), 308-329.
14. 2+, and the inhibitor pdTp, refined at 1.65 Å, Proteins: Struct. Funct. Genet. 5 (1989), 183-201.
15. G.E.O. Borgstahl, D.R. Williams and E.D. Getzoff, 1.4 Å structure of photoactive yellow protein, a cytosolic photoreceptor: Unusual fold, active site, and chromophore, Biochemistry 34 (1995), 6278-6287.
16. W.W. Sprenger, W.D. Hoff, J.P. Armitage and K.J. Hellingwerf, The eubacterium Ectothiorhodospira halophila is negatively phototactic, with a wavelength dependence that fits the absorption spectrum of the photoactive yellow protein, J. Bacteriol. 175 (1993), 3096-3104.