메뉴 건너뛰기




Volumn 37, Issue SUPPL. 3, 1999, Pages 186-193

Improved ab initio predictions with a simplified, flexible geometry model

Author keywords

Force field; Molecular dynamics; Protein folding; Secondary structure

Indexed keywords

PROTEIN;

EID: 0032620117     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(1999)37:3+<186::AID-PROT23>3.0.CO;2-D     Document Type: Article
Times cited : (29)

References (15)
  • 1
    • 0015859467 scopus 로고
    • Principles that govern the folding of polypeptide chains
    • Anfinsen C. Principles that govern the folding of polypeptide chains. Science 1973;181:223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.1
  • 2
    • 0031308499 scopus 로고    scopus 로고
    • Analysis of the predicted structures of domain 1 of protein G3 (T0030) and NK-Lysin (T0042)
    • Osguthorpe DJ. Analysis of the predicted structures of domain 1 of protein G3 (T0030) and NK-Lysin (T0042). Proteins Suppl 1997;1: 172-178.
    • (1997) Proteins Suppl , vol.1 , pp. 172-178
    • Osguthorpe, D.J.1
  • 3
    • 0028960071 scopus 로고
    • Role of electrostatic screening in determining protein main chain conformational preferences
    • Avbel F, Moult J. Role of electrostatic screening in determining protein main chain conformational preferences. Biochemistry 1995;34:755-764.
    • (1995) Biochemistry , vol.34 , pp. 755-764
    • Avbel, F.1    Moult, J.2
  • 4
    • 0026665778 scopus 로고
    • Side-chain entropy opposes alpha-helix formation but rationalizes experimentally determined helix-forming propensities
    • Creamer TP, Rose GD. Side-chain entropy opposes alpha-helix formation but rationalizes experimentally determined helix-forming propensities. Proc Natl Acad Sci USA 1992;89:5937-5941.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 5937-5941
    • Creamer, T.P.1    Rose, G.D.2
  • 5
    • 0031038377 scopus 로고    scopus 로고
    • Local interactions in protein folding: Lessons from the α-helix
    • Aurora R, Creamer TP, Srinivasan R, Rose GD. Local interactions in protein folding: lessons from the α-helix. J Biol Chem 1997;272: 1413-1416.
    • (1997) J Biol Chem , vol.272 , pp. 1413-1416
    • Aurora, R.1    Creamer, T.P.2    Srinivasan, R.3    Rose, G.D.4
  • 6
    • 0021813940 scopus 로고
    • On the calculation of electrostatic interactions in proteins
    • Gilson MK, Rashin A, Fine R, Honig B. On the calculation of electrostatic interactions in proteins. J Mol Biol 1985;183:503-516.
    • (1985) J Mol Biol , vol.183 , pp. 503-516
    • Gilson, M.K.1    Rashin, A.2    Fine, R.3    Honig, B.4
  • 9
    • 0344423627 scopus 로고    scopus 로고
    • Reference deleted in proofs
    • Reference deleted in proofs.
  • 10
    • 0025978283 scopus 로고
    • Database algorithm for generating protein backbone and side-chain coordinates from a C-alpha trace application to model-building and detection of coordinate errors
    • Holm L, Sande C. Database algorithm for generating protein backbone and side-chain coordinates from a C-alpha trace application to model-building and detection of coordinate errors. J Mol Biol 1991;218:183-194.
    • (1991) J Mol Biol , vol.218 , pp. 183-194
    • Holm, L.1    Sande, C.2
  • 11
    • 0027291015 scopus 로고
    • Prediction of secondary structure at better than 70% accuracy
    • Rost B, Sander C. Prediction of secondary structure at better than 70% accuracy. J Mol Biol 1993;232:584-599.
    • (1993) J Mol Biol , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 12
    • 0028300741 scopus 로고
    • Combining evolutionary information and neural networks to predict protein secondary structure
    • Rost B, Sander C. Combining evolutionary information and neural networks to predict protein secondary structure. Proteins 1994;19:55-72.
    • (1994) Proteins , vol.19 , pp. 55-72
    • Rost, B.1    Sander, C.2
  • 13
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl Cryst 1991;24:946-950.
    • (1991) J Appl Cryst , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 14
    • 0345286698 scopus 로고    scopus 로고
    • http://PredictionCenter.llnl.gov/casp3/results/th/
  • 15
    • 0345286697 scopus 로고    scopus 로고
    • http://PredictionCenter.Ilnl.gov/casp3/results/SS-browser/ pred_search.cgi


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.