메뉴 건너뛰기




Volumn 6, Issue 11, 2011, Pages

Revisiting the NMR structure of the ultrafast downhill folding protein GPW from bacteriophage λ

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; GPW PROTEIN; UNCLASSIFIED DRUG; PROTEIN W, BACTERIOPHAGE LAMBDA; VIRUS PROTEIN;

EID: 80455156128     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0026409     Document Type: Article
Times cited : (18)

References (25)
  • 1
    • 0034705482 scopus 로고    scopus 로고
    • Thermodynamic and functional characterization of protein W from bacteriophage lambda. The three C-terminal residues are critical for activity
    • Maxwell KL, Davidson AR, Murialdo H, Gold M, (2000) Thermodynamic and functional characterization of protein W from bacteriophage lambda. The three C-terminal residues are critical for activity. J Biol Chem 275: 18879-18886.
    • (2000) J Biol Chem , vol.275 , pp. 18879-18886
    • Maxwell, K.L.1    Davidson, A.R.2    Murialdo, H.3    Gold, M.4
  • 2
    • 0345258031 scopus 로고    scopus 로고
    • The product of the bacteriophage lambda W gene: purification and properties
    • Murialdo H, Xing X, Tzamtzis D, Haddad A, Gold M, (2003) The product of the bacteriophage lambda W gene: purification and properties. Biochem Cell Biol 81: 307-315.
    • (2003) Biochem Cell Biol , vol.81 , pp. 307-315
    • Murialdo, H.1    Xing, X.2    Tzamtzis, D.3    Haddad, A.4    Gold, M.5
  • 3
    • 0035917324 scopus 로고    scopus 로고
    • The solution structure of bacteriophage lambda protein W, a small morphogenetic protein possessing a novel fold
    • Maxwell KL, Yee AA, Booth V, Arrowsmith CH, Gold M, et al. (2001) The solution structure of bacteriophage lambda protein W, a small morphogenetic protein possessing a novel fold. J Mol Biol 308: 9-14.
    • (2001) J Mol Biol , vol.308 , pp. 9-14
    • Maxwell, K.L.1    Yee, A.A.2    Booth, V.3    Arrowsmith, C.H.4    Gold, M.5
  • 4
    • 44949091517 scopus 로고    scopus 로고
    • Expanding the realm of ultrafast protein folding: gpW, a midsize natural single-domain with alpha+beta topology that folds downhill
    • Fung A, Li P, Godoy-Ruiz R, Sanchez-Ruiz JM, Muñoz V, (2008) Expanding the realm of ultrafast protein folding: gpW, a midsize natural single-domain with alpha+beta topology that folds downhill. J Am Chem Soc 130: 7489-7495.
    • (2008) J Am Chem Soc , vol.130 , pp. 7489-7495
    • Fung, A.1    Li, P.2    Godoy-Ruiz, R.3    Sanchez-Ruiz, J.M.4    Muñoz, V.5
  • 5
    • 46449085241 scopus 로고    scopus 로고
    • Energy minimizations with a combination of two knowledge-based potentials for protein folding
    • de Sancho D, Rey A, (2008) Energy minimizations with a combination of two knowledge-based potentials for protein folding. J Comp Chem 29: 1684-1692.
    • (2008) J Comp Chem , vol.29 , pp. 1684-1692
    • de Sancho, D.1    Rey, A.2
  • 6
    • 79953684009 scopus 로고    scopus 로고
    • Quantitative prediction of protein folding behaviors from a simple statistical model
    • Bruscolini P, Naganathan AN, (2011) Quantitative prediction of protein folding behaviors from a simple statistical model. J Am Chem Soc 133: 5372-5379.
    • (2011) J Am Chem Soc , vol.133 , pp. 5372-5379
    • Bruscolini, P.1    Naganathan, A.N.2
  • 7
    • 33746102627 scopus 로고    scopus 로고
    • Atom-by-atom analysis of global downhill protein folding
    • Sadqi M, Fushman D, Muñoz V, (2006) Atom-by-atom analysis of global downhill protein folding. Nature 442: 317-321.
    • (2006) Nature , vol.442 , pp. 317-321
    • Sadqi, M.1    Fushman, D.2    Muñoz, V.3
  • 9
    • 0032857781 scopus 로고    scopus 로고
    • Automated analysis of NMR assignments and structures for proteins
    • Moseley HN, Montelione GT, (1999) Automated analysis of NMR assignments and structures for proteins. Curr Opin Struct Biol 9: 635-642.
    • (1999) Curr Opin Struct Biol , vol.9 , pp. 635-642
    • Moseley, H.N.1    Montelione, G.T.2
  • 10
    • 58149468410 scopus 로고    scopus 로고
    • De novo protein structure generation from incomplete chemical shift assignments
    • Shen Y, Vernon R, Baker D, Bax A, (2009) De novo protein structure generation from incomplete chemical shift assignments. J Biomol NMR 43: 63-78.
    • (2009) J Biomol NMR , vol.43 , pp. 63-78
    • Shen, Y.1    Vernon, R.2    Baker, D.3    Bax, A.4
  • 11
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR
    • Laskowski RA, Rullmannn JA, MacArthur MW, Kaptein R, Thornton JM, (1996) AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J Biomol NMR 8: 477-486.
    • (1996) J Biomol NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 12
    • 12044252858 scopus 로고
    • Methodological advances in protein NMR
    • Bax A, Grzesiek S, (1993) Methodological advances in protein NMR. Accounts Chem Res 26: 131-138.
    • (1993) Accounts Chem Res , vol.26 , pp. 131-138
    • Bax, A.1    Grzesiek, S.2
  • 14
    • 34547592557 scopus 로고    scopus 로고
    • MolProbity: all-atom contacts and structure validation for proteins and nucleic acids
    • Davis IW, Leaver-Fay A, Chen VB, Block JN, Kapral GJ, et al. (2007) MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res 35: W375-W383.
    • (2007) Nucleic Acids Res , vol.35 , pp. 375-383
    • Davis, I.W.1    Leaver-Fay, A.2    Chen, V.B.3    Block, J.N.4    Kapral, G.J.5
  • 15
    • 0029983371 scopus 로고    scopus 로고
    • T7 vectors with modified T7lac promoter for expression of proteins in Escherichia coli
    • Peranen J, Rikkonen M, Hyvonen M, Kaariainen L, (1996) T7 vectors with modified T7lac promoter for expression of proteins in Escherichia coli. Anal Biochem 236: 371-373.
    • (1996) Anal Biochem , vol.236 , pp. 371-373
    • Peranen, J.1    Rikkonen, M.2    Hyvonen, M.3    Kaariainen, L.4
  • 16
    • 0029400480 scopus 로고
    • NMRPipe: a multidimensional spectral processing system based on UNIX pipes
    • Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, et al. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6: 277-293.
    • (1995) J Biomol NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5
  • 17
    • 0000041361 scopus 로고
    • A common sense approach to peak picking two-, three- and four-dimensional spectra using automatic computer analysis of contour diagrams
    • Garrett DS, Powers R, Gronenborn AM, Clore GM, (1991) A common sense approach to peak picking two-, three- and four-dimensional spectra using automatic computer analysis of contour diagrams. J Magn Reson 95: 216-220.
    • (1991) J Magn Reson , vol.95 , pp. 216-220
    • Garrett, D.S.1    Powers, R.2    Gronenborn, A.M.3    Clore, G.M.4
  • 18
    • 68349093958 scopus 로고    scopus 로고
    • TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts
    • Shen Y, Delaglio F, Cornilescu G, Bax A, (2009) TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J Biomol NMR 44: 213-223.
    • (2009) J Biomol NMR , vol.44 , pp. 213-223
    • Shen, Y.1    Delaglio, F.2    Cornilescu, G.3    Bax, A.4
  • 20
    • 66749116183 scopus 로고    scopus 로고
    • DeLano, DeLano Scientific LLC, San Carlos, CA
    • DeLano (2004) The PyMOL Molecular Graphics System, DeLano Scientific LLC, San Carlos, CA.
    • (2004) The PyMOL Molecular Graphics System
  • 21
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess B, Kutzner C, van der Spoel D, Lindahl E, (2008) GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation. J Chem Theor Comp 4: 435-447.
    • (2008) J Chem Theor Comp , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    van der Spoel, D.3    Lindahl, E.4
  • 22
    • 77950106854 scopus 로고    scopus 로고
    • Implementation of the CHARMM force field in GROMACS: Analysis of protein stability effects from correction maps, virtual interaction sites, and water models
    • Bjelkmar Pr, Larsson P, Cuendet MA, Hess B, Lindahl E, (2010) Implementation of the CHARMM force field in GROMACS: Analysis of protein stability effects from correction maps, virtual interaction sites, and water models. J Chem Theor Comp 6: 459-466.
    • (2010) J Chem Theor Comp , vol.6 , pp. 459-466
    • Bjelkmar, P.1    Larsson, P.2    Cuendet, M.A.3    Hess, B.4    Lindahl, E.5
  • 23
    • 4544369164 scopus 로고
    • A generalized reaction field method for molecular dynamics simulations
    • Tironi IG, Sperb R, Smith PE, van Gunsteren WF, (1995) A generalized reaction field method for molecular dynamics simulations. J Chem Phys 102: 5451-5459.
    • (1995) J Chem Phys , vol.102 , pp. 5451-5459
    • Tironi, I.G.1    Sperb, R.2    Smith, P.E.3    van Gunsteren, W.F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.