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Volumn 93, Issue 1-2, 2008, Pages 78-89

Hydrophobic condensation and modular assembly model of protein folding

Author keywords

Hydrophobic condensation; Modular assembly model; Protein folding; Staphylococcal nuclease

Indexed keywords

GLOBULAR PROTEIN; PEPTIDE; STAPHYLOCOCCAL NUCLEASE;

EID: 46849118765     PISSN: 03032647     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biosystems.2008.04.007     Document Type: Article
Times cited : (8)

References (82)
  • 4
    • 0034604105 scopus 로고    scopus 로고
    • Baker D. Nature 405 (2000) 39-42
    • (2000) Nature , vol.405 , pp. 39-42
    • Baker, D.1
  • 5
    • 33644852931 scopus 로고    scopus 로고
    • Bates G.P. Science 311 (2006) 1385-1386
    • (2006) Science , vol.311 , pp. 1385-1386
    • Bates, G.P.1
  • 15
    • 85194557646 scopus 로고    scopus 로고
    • Chow, C.-Y., Wu, M.-C., Fang, H.-J., Hu, C.-K., Chen, H.-M., Tsong, T.-Y., 2008. Compact dimension of denatured states of staphylococcal nuclease. Proteins: Struct. Funct. Bioinf. 72, 901-909.
    • Chow, C.-Y., Wu, M.-C., Fang, H.-J., Hu, C.-K., Chen, H.-M., Tsong, T.-Y., 2008. Compact dimension of denatured states of staphylococcal nuclease. Proteins: Struct. Funct. Bioinf. 72, 901-909.
  • 16
    • 85194534430 scopus 로고    scopus 로고
    • Cohen, F.E., Kelly, J.W., 2003. Nature 426, 905-909.
    • Cohen, F.E., Kelly, J.W., 2003. Nature 426, 905-909.
  • 20
    • 0347357617 scopus 로고    scopus 로고
    • Dobson C.M. Nautre 426 (2003) 884-890
    • (2003) Nautre , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 33
  • 38
    • 85194584961 scopus 로고    scopus 로고
    • Hu, H.-Y., Wu, M.-C., Fang, H.-J., Forrest, M.D., Hu, C.-K., Tsong, T.-Y., Chen, H.-M. The role of tryptophan in staphylococcal nuclease stability, preprint.
    • Hu, H.-Y., Wu, M.-C., Fang, H.-J., Forrest, M.D., Hu, C.-K., Tsong, T.-Y., Chen, H.-M. The role of tryptophan in staphylococcal nuclease stability, preprint.
  • 39
    • 0004230174 scopus 로고
    • Elsevier/North-Holland Biomedical Press, Amsterdam
    • Jaenicke R. Protein Folding (1980), Elsevier/North-Holland Biomedical Press, Amsterdam
    • (1980) Protein Folding
    • Jaenicke, R.1
  • 64
    • 0002940127 scopus 로고
    • The molten globule state
    • Creighton T.E. (Ed), Freeman and Co., New York
    • Ptitsyn O.B. The molten globule state. In: Creighton T.E. (Ed). Protein Folding (1992), Freeman and Co., New York 243-300
    • (1992) Protein Folding , pp. 243-300
    • Ptitsyn, O.B.1
  • 65
    • 0017798828 scopus 로고
    • Rose G.D. Nature 272 (1978) 586-590
    • (1978) Nature , vol.272 , pp. 586-590
    • Rose, G.D.1
  • 68
    • 0347987853 scopus 로고    scopus 로고
    • Selkoe D.J. Nature 426 (2003) 900-904
    • (2003) Nature , vol.426 , pp. 900-904
    • Selkoe, D.J.1
  • 72
    • 0347987854 scopus 로고    scopus 로고
    • Smith A. Nature 426 (2003) 883
    • (2003) Nature , vol.426 , pp. 883
    • Smith, A.1
  • 79
    • 85194562528 scopus 로고    scopus 로고
    • Tsong, T.-Y., Su, Z.-D., 1999. AIP Conf. Proc. 487, 37-53.
    • Tsong, T.-Y., Su, Z.-D., 1999. AIP Conf. Proc. 487, 37-53.
  • 81
    • 0043180474 scopus 로고    scopus 로고
    • (The website of the protein sequence culling server is http://dunbrack.fccc.edu/pisces/. Here we used version cullpdb_pc20_res1.6_R0.25_d040724_chains743.)
    • Wang G., and Dunbrack Jr. R.L. Bioinformatics 19 (2003) 1589. http://dunbrack.fccc.edu/pisces/ (The website of the protein sequence culling server is http://dunbrack.fccc.edu/pisces/. Here we used version cullpdb_pc20_res1.6_R0.25_d040724_chains743.)
    • (2003) Bioinformatics , vol.19 , pp. 1589
    • Wang, G.1    Dunbrack Jr., R.L.2
  • 82
    • 85194575643 scopus 로고    scopus 로고
    • Wu, M.-C., Hu, C.-K., Chen, H.-M., Tsong, T.-Y. Local hydrophobicity and protein secondary structure formation: theoretical model and experimental test, preprint.
    • Wu, M.-C., Hu, C.-K., Chen, H.-M., Tsong, T.-Y. Local hydrophobicity and protein secondary structure formation: theoretical model and experimental test, preprint.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.