메뉴 건너뛰기




Volumn 74, Issue 6, 1998, Pages 3190-3197

Site-specific thermodynamics and kinetics of a coiled-coil transition by spin inversion transfer NMR

Author keywords

[No Author keywords available]

Indexed keywords

LEUCINE ZIPPER PROTEIN; SYNTHETIC PEPTIDE;

EID: 0031806728     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)78025-7     Document Type: Article
Times cited : (27)

References (18)
  • 1
    • 44949286565 scopus 로고
    • Bayesian analysis. I. Parameter estimation using quadrature NMR models
    • Bretthorst, G. L. 1990. Bayesian analysis. I. Parameter estimation using quadrature NMR models. J. Magn. Reson. 88:533-551.
    • (1990) J. Magn. Reson. , vol.88 , pp. 533-551
    • Bretthorst, G.L.1
  • 2
    • 0000553722 scopus 로고
    • Bayesian analysis. II. Model selection
    • Bretthorst, G. L. 1990a. Bayesian analysis. II. Model selection. J. Magn. Reson. 88:552-570.
    • (1990) J. Magn. Reson. , vol.88 , pp. 552-570
    • Bretthorst, G.L.1
  • 3
    • 44949266852 scopus 로고
    • Bayesian analysis. III. Applications to NMR signal detection, model selection, and parameter estimation
    • Bretthorst, G. L. 1990b. Bayesian analysis. III. Applications to NMR signal detection, model selection, and parameter estimation. J. Magn. Reson. 88:571-595.
    • (1990) J. Magn. Reson. , vol.88 , pp. 571-595
    • Bretthorst, G.L.1
  • 6
    • 0026317334 scopus 로고
    • Periodicity of amide proton exchange rates in a coiled-coil leucine zipper peptide
    • Goodman, E. M., and P. S. Kim. 1991. Periodicity of amide proton exchange rates in a coiled-coil leucine zipper peptide. Biochemistry. 30:11615-11620.
    • (1991) Biochemistry , vol.30 , pp. 11615-11620
    • Goodman, E.M.1    Kim, P.S.2
  • 7
    • 0028816067 scopus 로고
    • Structural stability of short subsequences of the tropomyosin chain
    • Holtzer, M. E., D. L. Crimmins, and A. Holtzer. 1995. Structural stability of short subsequences of the tropomyosin chain. Biopolymers. 35: 125-136.
    • (1995) Biopolymers , vol.35 , pp. 125-136
    • Holtzer, M.E.1    Crimmins, D.L.2    Holtzer, A.3
  • 8
    • 0012972120 scopus 로고
    • Does the unfolding transition of two-chain, coiled-coil proteins involve a continuum of intermediates?
    • L. M. Gierasch and J. King, editors. AAAS Books, Washington, D.C.
    • Holtzer, A., M. E. Holtzer, and J. Skolnick. 1990. Does the unfolding transition of two-chain, coiled-coil proteins involve a continuum of intermediates? In Protein Folding. L. M. Gierasch and J. King, editors. AAAS Books, Washington, D.C. 177-190.
    • (1990) Protein Folding , pp. 177-190
    • Holtzer, A.1    Holtzer, M.E.2    Skolnick, J.3
  • 10
    • 0029146297 scopus 로고
    • A calorimetric characterization of the salt dependence of the stability of the GCN4 leucine zipper
    • Kenar, K. T., B. Garcia-Moreno, and E. Freire. 1995. A calorimetric characterization of the salt dependence of the stability of the GCN4 leucine zipper. Protein Sci. 4:1934-1938.
    • (1995) Protein Sci. , vol.4 , pp. 1934-1938
    • Kenar, K.T.1    Garcia-Moreno, B.2    Freire, E.3
  • 12
    • 0030271515 scopus 로고    scopus 로고
    • Coiled coils: New structures and new functions
    • Lupas, A. 1996. Coiled coils: new structures and new functions. TIBS. 21:375-382.
    • (1996) TIBS , vol.21 , pp. 375-382
    • Lupas, A.1
  • 13
    • 0010957050 scopus 로고
    • Reaction rates by nuclear magnetic resonance
    • McConnell, H. M. 1958. Reaction rates by nuclear magnetic resonance. J. Chem. Phys. 28:430-431.
    • (1958) J. Chem. Phys. , vol.28 , pp. 430-431
    • McConnell, H.M.1
  • 14
    • 0016774265 scopus 로고
    • Tropomyosin coiled-coil interactions. Evidence for an unstaggered structure
    • McLachlan, A. D., and M. Stewart. 1975. Tropomyosin coiled-coil interactions. Evidence for an unstaggered structure. J. Mol. Biol. 98:293-304.
    • (1975) J. Mol. Biol. , vol.98 , pp. 293-304
    • McLachlan, A.D.1    Stewart, M.2
  • 15
    • 0026331267 scopus 로고
    • X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil
    • O'Shea, E. K., J. D. Klemm, P. S. Kim, and T. Alber. 1991. X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil. Science. 254:539-544.
    • (1991) Science , vol.254 , pp. 539-544
    • O'Shea, E.K.1    Klemm, J.D.2    Kim, P.S.3    Alber, T.4
  • 16
    • 0024534241 scopus 로고
    • Evidence that the leucine zipper is a coiled coil
    • O'Shea, E. K., R. Rutkowski, and P. S. Kim. 1989. Evidence that the leucine zipper is a coiled coil. Science. 243:538-542.
    • (1989) Science , vol.243 , pp. 538-542
    • O'Shea, E.K.1    Rutkowski, R.2    Kim, P.S.3
  • 17
    • 0020348367 scopus 로고
    • Stability of proteins: Proteins which do not present a single cooperative system
    • Privalov, P. L. 1982. Stability of proteins: proteins which do not present a single cooperative system. Adv. Protein Chem. 35:1-104.
    • (1982) Adv. Protein Chem. , vol.35 , pp. 1-104
    • Privalov, P.L.1
  • 18
    • 0000730907 scopus 로고
    • Measurement of reaction rates in vivo using magnetization transfer techniques
    • P. Diehl, E. Fluck, H. Günther, R. Kosfeld, and J. Seelig, editors.
    • Rudin, M., and A. Sauter. 1992. Measurement of reaction rates in vivo using magnetization transfer techniques. In NMR Basic Principles and Progress, P. Diehl, E. Fluck, H. Günther, R. Kosfeld, and J. Seelig, editors. 27:257-293.
    • (1992) NMR Basic Principles and Progress , vol.27 , pp. 257-293
    • Rudin, M.1    Sauter, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.