메뉴 건너뛰기




Volumn 41, Issue 1, 2008, Pages 29-41

Sequence specific resonance assignment via Multicanonical Monte Carlo search using an ABACUS approach

Author keywords

BACUS; Fragment Monte Carlo; NOE identification; Resonance assignment

Indexed keywords

PROTON;

EID: 43649085607     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-008-9238-2     Document Type: Article
Times cited : (34)

References (27)
  • 1
    • 0033677333 scopus 로고    scopus 로고
    • The NOESY jigsaw: Automated protein secondary structure and main-chain assignment from sparse, unassigned NMR data
    • Bailey-Kellogg C, Widge A, Kelley JJ, Berardi MJ, Bushweller JH, Donald BR (2000) The NOESY jigsaw: Automated protein secondary structure and main-chain assignment from sparse, unassigned NMR data. J Comput Biol 7:537-558
    • (2000) J Comput Biol , vol.7 , pp. 537-558
    • Bailey-Kellogg, C.1    Widge, A.2    Kelley, J.J.3    Berardi, M.J.4    Bushweller, J.H.5    Donald, B.R.6
  • 2
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
    • Bartels C, Xia T, Billeter M, Güntert P, Wuüthrich K (1995) The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J Biomol NMR 6:1-10
    • (1995) J Biomol NMR , vol.6 , pp. 1-10
    • Bartels, C.1    Xia, T.2    Billeter, M.3    Güntert, P.4    Wuüthrich, K.5
  • 3
    • 0000106469 scopus 로고
    • Multicanonical algorithms for first order phase transitions
    • Berg BA, Neuhaus T (1991) Multicanonical algorithms for first order phase transitions. Phys Lett B 267:249-253
    • (1991) Phys Lett B , vol.267 , pp. 249-253
    • Berg, B.A.1    Neuhaus, T.2
  • 4
    • 0001629677 scopus 로고
    • New approach to spin-glass simulation
    • Berg BA, Celik T (1992) New approach to spin-glass simulation. Phys Rev Lett 69:2292-2295
    • (1992) Phys Rev Lett , vol.69 , pp. 2292-2295
    • Berg, B.A.1    Celik, T.2
  • 7
    • 23544469152 scopus 로고
    • New Monte Carlo technique for studing phase transitions
    • Ferrenberg AM, Swendsen RH (1989) New Monte Carlo technique for studing phase transitions. Phys Rev Lett 63:1658
    • (1989) Phys Rev Lett , vol.63 , pp. 1658
    • Ferrenberg, A.M.1    Swendsen, R.H.2
  • 9
    • 0037076277 scopus 로고    scopus 로고
    • CLOUDS, a protocol for deriving a molecular proton density via NMR
    • Grishaev A, Llinás M (2002a) CLOUDS, a protocol for deriving a molecular proton density via NMR. Proc Natl Acad Sci USA 99:6707-6712
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 6707-6712
    • Grishaev, A.1    Llinás, M.2
  • 10
    • 0037076350 scopus 로고    scopus 로고
    • Protein structure elucidation from NMR proton density
    • Grishaev A, Llinás M (2002b) Protein structure elucidation from NMR proton density. Proc Natl Acad Sci USA 99:6713-6718
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 6713-6718
    • Grishaev, A.1    Llinás, M.2
  • 11
    • 1242295376 scopus 로고    scopus 로고
    • BACUS: A Bayesian protocol for the identification of protein NOESY spectra via unassigned spin systems
    • Grishaev A, Llinás M (2004) BACUS: A Bayesian protocol for the identification of protein NOESY spectra via unassigned spin systems. J Biomol NMR 28:1-10
    • (2004) J Biomol NMR , vol.28 , pp. 1-10
    • Grishaev, A.1    Llinás, M.2
  • 13
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Güntert P, Mumenthaler C, Wüthrich K (1997) Torsion angle dynamics for NMR structure calculation with the new program DYANA. J Mol Biol 273:283-298
    • (1997) J Mol Biol , vol.273 , pp. 283-298
    • Güntert, P.1    Mumenthaler, C.2    Wüthrich, K.3
  • 14
    • 4644340524 scopus 로고    scopus 로고
    • Automated NMR structure calculation with CYANA
    • Güntert P (2004) Automated NMR structure calculation with CYANA. Methods Mol Biol 278:353-378
    • (2004) Methods Mol Biol , vol.278 , pp. 353-378
    • Güntert, P.1
  • 15
    • 5244260010 scopus 로고
    • Prediction of peptide conformation by multicanonical algorithm: New approach to the multiple-minima problem
    • Hansmann UH, Okamoto Y (1993) Prediction of peptide conformation by multicanonical algorithm: New approach to the multiple-minima problem. J Comp Chem 14:1333-1338
    • (1993) J Comp Chem , vol.14 , pp. 1333-1338
    • Hansmann, U.H.1    Okamoto, Y.2
  • 16
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • Herrmann T, Güntert P, Wüthrich K (2002) Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J Mol Biol 319:209-227
    • (2002) J Mol Biol , vol.319 , pp. 209-227
    • Herrmann, T.1    Güntert, P.2    Wüthrich, K.3
  • 17
    • 34249674388 scopus 로고    scopus 로고
    • The conserved CPH domains of Cul7 and PARC are protein-protein interaction modules that bind the tetramerization domain of p53
    • Kaustov L, Lukin J, Lemak A, Duan S, Ho M, Doherty R, Penn LZ, Arrowsmith CH (2007) The conserved CPH domains of Cul7 and PARC are protein-protein interaction modules that bind the tetramerization domain of p53. J Biol Chem 282:11300-11307
    • (2007) J Biol Chem , vol.282 , pp. 11300-11307
    • Kaustov, L.1    Lukin, J.2    Lemak, A.3    Duan, S.4    Ho, M.5    Doherty, R.6    Penn, L.Z.7    Arrowsmith, C.H.8
  • 18
    • 19944411144 scopus 로고    scopus 로고
    • High-throughput analysis of protein NMR spectra
    • Malmodin D, Billeter M (2005) High-throughput analysis of protein NMR spectra. Progr NMR Spectrosc 46:109-129
    • (2005) Progr NMR Spectrosc , vol.46 , pp. 109-129
    • Malmodin, D.1    Billeter, M.2
  • 20
    • 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
  • 21
    • 34250373696 scopus 로고    scopus 로고
    • Sequence Specific resonance assignment of a hypothetical protein PA0128 from pseudomonas aeruginosa
    • Srisailam S, Lukin JA, Lemak A, Yee A, Arrowsmith CH (2006) Sequence Specific resonance assignment of a hypothetical protein PA0128 from pseudomonas aeruginosa. J Biomol NMR 36:27
    • (2006) J Biomol NMR , vol.36 , pp. 27
    • Srisailam, S.1    Lukin, J.A.2    Lemak, A.3    Yee, A.4    Arrowsmith, C.H.5
  • 22
    • 0025829776 scopus 로고
    • Refinement of the main chain directed assignment strategy for the analysis of 1H NMR spectra of proteins
    • Wand AJ, Nelson SJ (1991) Refinement of the main chain directed assignment strategy for the analysis of 1H NMR spectra of proteins. Biophys J 59:1101-1112
    • (1991) Biophys J , vol.59 , pp. 1101-1112
    • Wand, A.J.1    Nelson, S.J.2
  • 24
    • 0033614004 scopus 로고    scopus 로고
    • Asparagine and glutamine: Using hydrogen atom contacts in the choice of side-chain amide orientation
    • Word JM, Lovell SC, Richardson JS, Richardson DC (1999) Asparagine and glutamine: Using hydrogen atom contacts in the choice of side-chain amide orientation. J Mol Biol 285:1735-1747
    • (1999) J Mol Biol , vol.285 , pp. 1735-1747
    • Word, J.M.1    Lovell, S.C.2    Richardson, J.S.3    Richardson, D.C.4
  • 27
    • 0028883616 scopus 로고
    • Automated analysis of nuclear magnetic resonance assignment for proteins
    • Zimmerman DE, Montelione GT (1995) Automated analysis of nuclear magnetic resonance assignment for proteins. Curr Opin Struct Biol 5:664-673
    • (1995) Curr Opin Struct Biol , vol.5 , pp. 664-673
    • Zimmerman, D.E.1    Montelione, G.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.