메뉴 건너뛰기




Volumn 580, Issue 22, 2006, Pages 5263-5267

Topological accessibility shows a distinct asymmetry in the folds of βα proteins

Author keywords

Fold asymmetry; N terminal folding; Protein topology

Indexed keywords

PROTEIN DERIVATIVE;

EID: 33748796668     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2006.08.070     Document Type: Article
Times cited : (14)

References (14)
  • 1
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • Richardson J.S. The anatomy and taxonomy of protein structure. Adv. Prot. Chem. 34 (1981) 167-339
    • (1981) Adv. Prot. Chem. , vol.34 , pp. 167-339
    • Richardson, J.S.1
  • 2
    • 0028181017 scopus 로고
    • An algorithm for automatically generating protein topology cartoons
    • Flores T.P., Moss D.S., and Thornton J.M. An algorithm for automatically generating protein topology cartoons. Prot. Engng. 7 (1994) 31-37
    • (1994) Prot. Engng. , vol.7 , pp. 31-37
    • Flores, T.P.1    Moss, D.S.2    Thornton, J.M.3
  • 3
    • 0037061460 scopus 로고    scopus 로고
    • A periodic table for protein structure
    • Taylor W.R. A periodic table for protein structure. Nature 416 (2002) 657-660
    • (2002) Nature , vol.416 , pp. 657-660
    • Taylor, W.R.1
  • 5
    • 0034604105 scopus 로고    scopus 로고
    • A surprising simplicity to protein folding
    • Baker D. A surprising simplicity to protein folding. Nature 405 (2000) 39-42
    • (2000) Nature , vol.405 , pp. 39-42
    • Baker, D.1
  • 6
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement and the refolding rates of single domain proteins
    • Plaxco K.W., Simons K.T., and Baker D. Contact order, transition state placement and the refolding rates of single domain proteins. J. Mol. Biol. 277 (1998) 985-994
    • (1998) J. Mol. Biol. , vol.277 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.T.2    Baker, D.3
  • 7
    • 17144369578 scopus 로고    scopus 로고
    • Protein folding rates estimated from contact predictions
    • Punta M., and Rost B. Protein folding rates estimated from contact predictions. J. Mol. Biol. 348 (2005) 507-512
    • (2005) J. Mol. Biol. , vol.348 , pp. 507-512
    • Punta, M.1    Rost, B.2
  • 8
    • 0034710671 scopus 로고    scopus 로고
    • A deeply knotted protein and how it might fold
    • Taylor W.R. A deeply knotted protein and how it might fold. Nature 406 (2000) 916-919
    • (2000) Nature , vol.406 , pp. 916-919
    • Taylor, W.R.1
  • 10
    • 0028961335 scopus 로고
    • SCOP: a structural classification of proteins database for the investigation of sequences and structures
    • Murzin A.G., Brenner S.E., Hubbard T., and Chothia C. SCOP: a structural classification of proteins database for the investigation of sequences and structures. J. Mol. Biol. 247 (1995) 536-540
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 11
    • 0029789824 scopus 로고    scopus 로고
    • A minimal gene set for cellular life derived by comparison of complete bacterial genomes
    • Mushegian A.R., and Koonin E.V. A minimal gene set for cellular life derived by comparison of complete bacterial genomes. Proc. Natl. Acad. Sci. USA 93 (1996) 10268-10273
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10268-10273
    • Mushegian, A.R.1    Koonin, E.V.2
  • 13
    • 0032924105 scopus 로고    scopus 로고
    • Chaperone-mediated protein folding
    • Fink A.L. Chaperone-mediated protein folding. Physiol. Rev. 79 (1999) 425-449
    • (1999) Physiol. Rev. , vol.79 , pp. 425-449
    • Fink, A.L.1
  • 14
    • 0013971370 scopus 로고
    • The three-dimensional structure of an enzyme
    • Phillips D.C. The three-dimensional structure of an enzyme. Sci. Am. 215 (1966) 78-90
    • (1966) Sci. Am. , vol.215 , pp. 78-90
    • Phillips, D.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.