메뉴 건너뛰기




Volumn 29, Issue SUPPL. 1, 1997, Pages 172-178

Analysis of the predicted structures of domain 1 of protein g3 (T0030) and NK-lysin (T0042)

Author keywords

Force field; Molecular dynamics; Protein folding; Secondary structure

Indexed keywords

PROTEIN; LUNG SURFACTANT; NK LYSIN; NK-LYSIN; PROTEOLIPID;

EID: 0031308499     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(sici)1097-0134(1997)1+<172::aid-prot22>3.0.co;2-k     Document Type: Article
Times cited : (5)

References (26)
  • 1
    • 0015859467 scopus 로고
    • Principles that govern the folding of polypeptide chains
    • Anfinsen, C. Principles that govern the folding of polypeptide chains. Science 181:223-230, 1973.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.1
  • 2
    • 0023769808 scopus 로고
    • Structure and energetics of ligand binding to proteins: Escherichia coli dihydrofolate reductase-trimethoprim, a drug-receptor system
    • Dauber-Osguthorpe, P., Roberts, V.A., Osguthorpe, D.J., Wolff, J., Genest, M., and Hagler, A.T. Structure and energetics of ligand binding to proteins: Escherichia coli dihydrofolate reductase-trimethoprim, a drug-receptor system. Proteins 4:31-47, 1988.
    • (1988) Proteins , vol.4 , pp. 31-47
    • Dauber-Osguthorpe, P.1    Roberts, V.A.2    Osguthorpe, D.J.3    Wolff, J.4    Genest, M.5    Hagler, A.T.6
  • 5
    • 0028949547 scopus 로고
    • Theoretical studies of protein folding and unfolding
    • Karplus, M. and Sali, A. Theoretical studies of protein folding and unfolding. Curr. Opin. Struct. Biol. 5:58-73, 1995.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 58-73
    • Karplus, M.1    Sali, A.2
  • 6
    • 0002970457 scopus 로고
    • Conformational searching using simulated annealing
    • K.M. Merz Jr. and S.M. Le Grand, eds. Birkhauser, Boston
    • Wilson, S.R. and Culi, W. Conformational searching using simulated annealing. In: "The Protein Folding Problem and Tertiary Structure Prediction." K.M. Merz Jr. and S.M. Le Grand, eds. Birkhauser, Boston, 1994:43-70.
    • (1994) The Protein Folding Problem and Tertiary Structure Prediction , pp. 43-70
    • Wilson, S.R.1    Culi, W.2
  • 7
    • 0003682904 scopus 로고
    • The genetic algorithm and protein tertiary structure prediction
    • K.M. Merz Jr. and S.M. Le Grand, eds. Birkhauser, Boston
    • Le Grand, S.M. and Merz, K.M. Jr., The genetic algorithm and protein tertiary structure prediction. In: "The Protein Folding Problem and Tertiary Structure Prediction." K.M. Merz Jr. and S.M. Le Grand, eds. Birkhauser, Boston, 1994:109-123.
    • (1994) The Protein Folding Problem and Tertiary Structure Prediction , pp. 109-123
    • Le Grand, S.M.1    Merz Jr., K.M.2
  • 8
    • 0011804246 scopus 로고
    • Molecular dynamics studies of protein and peptide folding and unfolding
    • K.M. Merz Jr. and S.M. Le Grand, eds. Birkhauser, Boston
    • Caflisch, A. and Karplus, M. Molecular dynamics studies of protein and peptide folding and unfolding. In: "The Protein Folding Problem and Tertiary Structure Prediction." K.M. Merz Jr. and S.M. Le Grand, eds. Birkhauser, Boston, 1994:193-230.
    • (1994) The Protein Folding Problem and Tertiary Structure Prediction , pp. 193-230
    • Caflisch, A.1    Karplus, M.2
  • 10
    • 0017873321 scopus 로고
    • Analysis of accuracy and implications of simple methods for predicting secondary structure of globular proteins
    • Garnier, J., Osguthorpe, D.J. and Robson, B. Analysis of accuracy and implications of simple methods for predicting secondary structure of globular proteins. J. Mol. Biol. 120:97-120, 1978.
    • (1978) J. Mol. Biol. , vol.120 , pp. 97-120
    • Garnier, J.1    Osguthorpe, D.J.2    Robson, B.3
  • 11
    • 0029000696 scopus 로고
    • Knowledge based potentials for proteins
    • Sippl, M. Knowledge based potentials for proteins. Curr. Opin. Struct. Biol. 5:229-235, 1995.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 229-235
    • Sippl, M.1
  • 13
    • 0016610491 scopus 로고
    • Computer simulation of protein folding
    • Levitt, M. and Warshel, A. Computer simulation of protein folding. Nature 253:694-698, 1975.
    • (1975) Nature , vol.253 , pp. 694-698
    • Levitt, M.1    Warshel, A.2
  • 14
    • 0006399208 scopus 로고
    • On the formation of protein tertiary structure on a computer
    • Hagler, A.T. and Honig, B. On the formation of protein tertiary structure on a computer. Proc. Natl. Acad. Sci. USA 75:554, 1978.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 554
    • Hagler, A.T.1    Honig, B.2
  • 15
    • 0028203492 scopus 로고
    • Monte carlo simulations of protein folding. I. Lattice model and interaction scheme
    • Kolinski, A. and Skolnick, J. Monte carlo simulations of protein folding. I. Lattice model and interaction scheme. Proteins 18:338-352, 1994.
    • (1994) Proteins , vol.18 , pp. 338-352
    • Kolinski, A.1    Skolnick, J.2
  • 16
    • 0028897718 scopus 로고
    • Computer modelling of protein folding: Conformational and energetic analysis of reduced and detailed protein models
    • Monge, A., Lathrop, E.J.P., Gunn, J.R., Shenkin, P.S. and Friesner, R.A. Computer modelling of protein folding: Conformational and energetic analysis of reduced and detailed protein models. J. Mol. Biol. 247:995-1012, 1995.
    • (1995) J. Mol. Biol. , vol.247 , pp. 995-1012
    • Monge, A.1    Lathrop, E.J.P.2    Gunn, J.R.3    Shenkin, P.S.4    Friesner, R.A.5
  • 17
    • 33947468892 scopus 로고
    • Theory of protein titration curves. I. General equations for impenetrable spheres
    • Tanford, C. and Kirkwood, J.G. Theory of protein titration curves. I. General equations for impenetrable spheres. J. Am. Chem. Soc. 79:5333-5339, 1957.
    • (1957) J. Am. Chem. Soc. , vol.79 , pp. 5333-5339
    • Tanford, C.1    Kirkwood, J.G.2
  • 20
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24:946-950, 1991.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 21
    • 0028297304 scopus 로고
    • Folding the main chain of small proteins with the genetic algorithm
    • Dandekar, T. and Argos, P. Folding the main chain of small proteins with the genetic algorithm. J. Mol. Biol. 236:844-861, 1994.
    • (1994) J. Mol. Biol. , vol.236 , pp. 844-861
    • Dandekar, T.1    Argos, P.2
  • 23
    • 0028354429 scopus 로고
    • Two crystal structures of the B1 immunoglobin-binding domain of streptococcal protein-G and comparison with NMR
    • Gallagher, T., Alexander, P., Bryan, P. and Gilliland, G.L. Two crystal structures of the B1 immunoglobin-binding domain of streptococcal protein-G and comparison with NMR. Biochemistry 33:4721-4729, 1994.
    • (1994) Biochemistry , vol.33 , pp. 4721-4729
    • Gallagher, T.1    Alexander, P.2    Bryan, P.3    Gilliland, G.L.4
  • 24
    • 0031038377 scopus 로고    scopus 로고
    • Local interactions in protein folding: Lessons from the α-helix
    • Aurora, R., Creamer, T.P., Srinivasan, R. and Rose, G.D. Local interactions in protein folding: Lessons from the α-helix. J. Biol. Chem. 272:1413-1416, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1413-1416
    • Aurora, R.1    Creamer, T.P.2    Srinivasan, R.3    Rose, G.D.4
  • 25
    • 0028960071 scopus 로고
    • Role of electrostatic screening in determining protein main chain conformational preferences
    • Avbelj, F. and Moult, J. Role of electrostatic screening in determining protein main chain conformational preferences. Biochemistry 34:755-764, 1995.
    • (1995) Biochemistry , vol.34 , pp. 755-764
    • Avbelj, F.1    Moult, J.2
  • 26
    • 0026665778 scopus 로고
    • Side-chain entropy opposes alpha-helix formation but rationalizes experimentally determined helix-forming propensities
    • Creamer, T.P. and Rose, G.D. Side-chain entropy opposes alpha-helix formation but rationalizes experimentally determined helix-forming propensities. Proc. Natl. Acad. Sci. USA 89:5937-5941, 1992.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5937-5941
    • Creamer, T.P.1    Rose, G.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.