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Volumn 6, Issue 7, 2011, Pages

Modeling disordered regions in proteins using Rosetta

Author keywords

[No Author keywords available]

Indexed keywords

ALGORITHM; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; COMPUTER PROGRAM; CONTROLLED STUDY; ENTROPY; METHODOLOGY; MOLECULAR MODEL; NUCLEAR MAGNETIC RESONANCE; PREDICTION; PROCESS OPTIMIZATION; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; X RAY CRYSTALLOGRAPHY; AMINO ACID SEQUENCE; BIOLOGY; CHEMICAL STRUCTURE; CHEMISTRY; HUMAN; METABOLISM; MOLECULAR GENETICS;

EID: 79960930163     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0022060     Document Type: Article
Times cited : (24)

References (11)
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  • 2
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    • Coupled folding and binding with alpha-helix-forming molecular recognition elements
    • Oldfield CJ, Yugong C, Cortese MS, Romero P, Uversky V, et al. (2005) Coupled folding and binding with alpha-helix-forming molecular recognition elements. Biochemistry 44 (37): 12454-70.
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  • 5
    • 78650905964 scopus 로고    scopus 로고
    • Rosetta3: an object oriented suite for the simulation and design of macromolecules
    • Leaver-Fay A, Tyka M, Lewis SM, Lange OF, Thompson J, et al. (2011) Rosetta3: an object oriented suite for the simulation and design of macromolecules. Methods Enzymol 487: 545-574.
    • (2011) Methods Enzymol , vol.487 , pp. 545-574
    • Leaver-Fay, A.1    Tyka, M.2    Lewis, S.M.3    Lange, O.F.4    Thompson, J.5
  • 6
    • 0033613255 scopus 로고    scopus 로고
    • Prediction of protein-folding mechanisms from free0energy landscapes derived from native structures
    • Alm E, Baker D, (1999) Prediction of protein-folding mechanisms from free0energy landscapes derived from native structures. Proc Natl Acad Sci USA 96: 11305-11310.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 11305-11310
    • Alm, E.1    Baker, D.2
  • 7
    • 0032605828 scopus 로고    scopus 로고
    • Processing and analysis of CASP3 protein structure predictions
    • Zemla A, Venclovas C, Moult J, Fidelis K, (1999) Processing and analysis of CASP3 protein structure predictions. Proteins: Struct Funct Genet 37 (Suppl 3): 22-29.
    • (1999) Proteins: Struct Funct Genet , vol.37 , Issue.SUPPL. 3 , pp. 22-29
    • Zemla, A.1    Venclovas, C.2    Moult, J.3    Fidelis, K.4
  • 8
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • Ward JJ, Sodhi JS, McGuffin LJ, Buxton BF, Jones DT, (2004) Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J of Mol Biol 337: 635-645.
    • (2004) J of Mol Biol , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 9
    • 42449146665 scopus 로고    scopus 로고
    • Consistent blind protein structure generation from NMR chemical shift data
    • Shen Y, Lange O, Delaglio F, Rossi P, Aramini J, et al. (2008) Consistent blind protein structure generation from NMR chemical shift data. Proc Natl Acad Sci USA 105: 4685-4690.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 4685-4690
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  • 10
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    • 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.
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    • A Simple Method To Predict Protein Flexibility Using Secondary Chemical Shifts
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.