메뉴 건너뛰기




Volumn 293, Issue 4, 1999, Pages 763-768

Submillisecond folding of the peripheral subunit-binding domain

Author keywords

Fast folding; Kinetics; NMR lineshape analysis; Protein folding; Two state folding

Indexed keywords

AMINO ACID SEQUENCE; ARTICLE; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN LOCALIZATION; TECHNIQUE; TEMPERATURE;

EID: 0033527587     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3189     Document Type: Article
Times cited : (75)

References (19)
  • 3
    • 0029151158 scopus 로고
    • Submillisecond folding of monomeric λ repressor
    • Huang G. S., Oas T. G. Submillisecond folding of monomeric λ repressor. Proc. Natl Acad. Sci. USA. 92:1995;6878-6882.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 6878-6882
    • Huang, G.S.1    Oas, T.G.2
  • 4
    • 0031815749 scopus 로고    scopus 로고
    • How do small single-domain proteins fold?
    • Jackson S. E. How do small single-domain proteins fold? Fold. Des. 3:1998;R81-R91.
    • (1998) Fold. Des. , vol.3
    • Jackson, S.E.1
  • 5
    • 0027404572 scopus 로고
    • The high-resolution structure of the peripheral subunit-binding domain from the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus
    • Kalia Y. N., Brocklehurst S. M., Hipps D. S., Appella E., Sakaguchi K., Perham R. N. The high-resolution structure of the peripheral subunit-binding domain from the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus. J. Mol. Biol. 230:1993;323-341.
    • (1993) J. Mol. Biol. , vol.230 , pp. 323-341
    • Kalia, Y.N.1    Brocklehurst, S.M.2    Hipps, D.S.3    Appella, E.4    Sakaguchi, K.5    Perham, R.N.6
  • 6
    • 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. Crystallog. 24:1991;946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 7
    • 0032545150 scopus 로고    scopus 로고
    • Global analysis of the effects of temperature and denaturant on the folding and unfolding kinetics of the N-terminal domain of the protein L9
    • Kuhlman B., Luisi D. L., Evans P. A., Raleigh D. P. Global analysis of the effects of temperature and denaturant on the folding and unfolding kinetics of the N-terminal domain of the protein L9. J. Mol. Biol. 284:1998;1661-1670.
    • (1998) J. Mol. Biol. , vol.284 , pp. 1661-1670
    • Kuhlman, B.1    Luisi, D.L.2    Evans, P.A.3    Raleigh, D.P.4
  • 8
    • 0030584659 scopus 로고    scopus 로고
    • Protein-protein interactions in the pyruvate dehydrogenase multienzyme complex: Dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetyltransferase
    • Mande S. S., Sarfaty S., Allen M. D., Perham R. N., Hol W. G. J. Protein-protein interactions in the pyruvate dehydrogenase multienzyme complex: dihydrolipoamide dehydrogenase complexed with the binding domain of the dihydrolipoamide acetyltransferase. Structure. 4:1996;277-286.
    • (1996) Structure , vol.4 , pp. 277-286
    • Mande, S.S.1    Sarfaty, S.2    Allen, M.D.3    Perham, R.N.4    Hol, W.G.J.5
  • 9
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement and the refolding rates of single domain protiens
    • Plaxco K. W., Simons K. T., Baker D. Contact order, transition state placement and the refolding rates of single domain protiens. J. Mol. Biol. 277:1998a;985-994.
    • (1998) J. Mol. Biol. , vol.277 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.T.2    Baker, D.3
  • 10
    • 85030367562 scopus 로고    scopus 로고
    • The Protein Society 12th Symposium, San Diego, CA
    • Plaxco K. W., Simons K. T., Baker D. The Protein Society 12th Symposium, San Diego, CA. Protein Sci. 7(suppl. 1):1998b;96.
    • (1998) Protein Sci. , vol.71 , pp. 96
    • Plaxco, K.W.1    Simons, K.T.2    Baker, D.3
  • 11
    • 33845561778 scopus 로고
    • Calibration of methanol and ethylene glycol nuclear magnetic resonance thermometers
    • Raiford D. S., Fisk C. L., Becker E. D. Calibration of methanol and ethylene glycol nuclear magnetic resonance thermometers. Anal. Chem. 51:1979;2050-2051.
    • (1979) Anal. Chem. , vol.51 , pp. 2050-2051
    • Raiford, D.S.1    Fisk, C.L.2    Becker, E.D.3
  • 12
    • 0033608968 scopus 로고    scopus 로고
    • Folding of the multidomain ribosomal protein L9: The two domains fold independently with remarkably different rates
    • Sato S., Kuhlman B., Wu W.-J., Raleigh D. P. Folding of the multidomain ribosomal protein L9: the two domains fold independently with remarkably different rates. Biochemistry. 38:1999;5643-5650.
    • (1999) Biochemistry , vol.38 , pp. 5643-5650
    • Sato, S.1    Kuhlman, B.2    Wu, W.-J.3    Raleigh, D.P.4
  • 14
    • 0032548905 scopus 로고    scopus 로고
    • Cooperative folding of a protein mini domain: The peripheral subunit-binding domain of the pyruvate dehydrogenase multienzyme complex
    • Spector S., Kuhlman B., Fairman R., Wong E., Boice J. A., Raleigh D. P. Cooperative folding of a protein mini domain: the peripheral subunit-binding domain of the pyruvate dehydrogenase multienzyme complex. J. Mol. Biol. 276:1998;479-489.
    • (1998) J. Mol. Biol. , vol.276 , pp. 479-489
    • Spector, S.1    Kuhlman, B.2    Fairman, R.3    Wong, E.4    Boice, J.A.5    Raleigh, D.P.6
  • 15
    • 0033616732 scopus 로고    scopus 로고
    • Nativelike structure and stability in a truncation mutant of a protein mini-domain: The peripheral subunit-binding domain
    • Spector S., Young P., Raleigh D. P. Nativelike structure and stability in a truncation mutant of a protein mini-domain: the peripheral subunit-binding domain. Biochemistry. 38:1999;4128-4136.
    • (1999) Biochemistry , vol.38 , pp. 4128-4136
    • Spector, S.1    Young, P.2    Raleigh, D.P.3
  • 16
    • 0030606223 scopus 로고    scopus 로고
    • Titration properties and thermodynamics of the transition state for folding: Comparison of two-state and multi-state folding pathways
    • Tan Y.-J., Oliveberg M., Fersht A. R. Titration properties and thermodynamics of the transition state for folding: comparison of two-state and multi-state folding pathways. J. Mol. Biol. 264:1996;377-389.
    • (1996) J. Mol. Biol. , vol.264 , pp. 377-389
    • Tan, Y.-J.1    Oliveberg, M.2    Fersht, A.R.3
  • 17
    • 0000050196 scopus 로고
    • From minimal models to real proteins: Time scales for protein folding kinetics
    • Thirumalai D. From minimal models to real proteins: time scales for protein folding kinetics. J. Phys. I (France). 5:1995;1457-1467.
    • (1995) J. Phys. I (France) , vol.5 , pp. 1457-1467
    • Thirumalai, D.1
  • 19


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.