메뉴 건너뛰기




Volumn 80, Issue 3, 2001, Pages 1466-1472

Conformational disorder of proteins assessed by real-space molecular dynamics refinement

Author keywords

[No Author keywords available]

Indexed keywords

ANISOTROPY; ARTICLE; CATALYSIS; CONFORMATIONAL TRANSITION; CRYSTALLOGRAPHY; DATA ANALYSIS; MACROMOLECULE; MOLECULAR DYNAMICS; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN STRUCTURE; X RAY DIFFRACTION;

EID: 0035118738     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(01)76118-8     Document Type: Article
Times cited : (13)

References (16)
  • 1
    • 0030986177 scopus 로고    scopus 로고
    • Cross-validated maximum-likelihood enhances simulated annealing crystallographic refinement
    • Adams, P. D., N. S. Pannu, R. J. Read, and A. T. Brünger. 1997. Cross-validated maximum-likelihood enhances simulated annealing crystallographic refinement. Proc. Natl. Acad. Sci. U.S.A. 94:5018-5023.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 5018-5023
    • Adams, P.D.1    Pannu, N.S.2    Read, R.J.3    Brünger, A.T.4
  • 3
    • 0001031179 scopus 로고
    • Proteins: A theoretical perspective of dynamics, structure and thermodynamics
    • Brooks, C. L., M. Karplus, and B. M. Pettitt. 1988. Proteins: a theoretical perspective of dynamics, structure and thermodynamics. Adv. Chem. Phys. 71:7-21.
    • (1988) Adv. Chem. Phys. , vol.71 , pp. 7-21
    • Brooks, C.L.1    Karplus, M.2    Pettitt, B.M.3
  • 4
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A. T. 1992. Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature. 355:472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 5
    • 0030767713 scopus 로고    scopus 로고
    • The free R value: A more objective statistic for crystallography
    • Brünger, A. T. 1997. The free R value: a more objective statistic for crystallography. Methods Enzymol. 277:366-396.
    • (1997) Methods Enzymol. , vol.277 , pp. 366-396
    • Brünger, A.T.1
  • 7
    • 0023140814 scopus 로고
    • Crystallographic R factor refinement by molecular dynamics
    • Brünger, A. T., J. Kuriyan, and M. Karplus. 1987. Crystallographic R factor refinement by molecular dynamics. Science. 235:458-460.
    • (1987) Science , vol.235 , pp. 458-460
    • Brünger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 8
    • 0033081171 scopus 로고    scopus 로고
    • Real space molecular dynamics refinement
    • Chen, Z., E. Blanc, and M. S. Chapman. 1999b. Real space molecular dynamics refinement. Acta Crystallogr. D55:464-468.
    • (1999) Acta Crystallogr. , vol.D55 , pp. 464-468
    • Chen, Z.1    Blanc, E.2    Chapman, M.S.3
  • 9
    • 0028078188 scopus 로고
    • Cross-validation tests of time-averaged molecular dynamics refinements for determination of protein structures by protein crystallography
    • Clarage, J. B., and G. N. Phillips. 1994. Cross-validation tests of time-averaged molecular dynamics refinements for determination of protein structures by protein crystallography. Acta Crystallogr. D50:24-36.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 24-36
    • Clarage, J.B.1    Phillips, G.N.2
  • 10
    • 84964589206 scopus 로고
    • Interferenz von Röntgenstrahlen und Wärmebewegung
    • Debye, P. 1912. Interferenz von Röntgenstrahlen und Wärmebewegung. Ann. Phys. 43:49-95.
    • (1912) Ann. Phys. , vol.43 , pp. 49-95
    • Debye, P.1
  • 11
    • 0025173665 scopus 로고
    • Inclusion of thermal motion in crystallographic structures by restrained molecular dynamics
    • Gros, P., W. F. van Gunsteren, and W. G. J. Hol. 1990. Inclusion of thermal motion in crystallographic structures by restrained molecular dynamics. Science. 249:1149-1152.
    • (1990) Science , vol.249 , pp. 1149-1152
    • Gros, P.1    Van Gunsteren, W.F.2    Hol, W.G.J.3
  • 12
    • 0022333121 scopus 로고
    • Stereochemically restrained refinement of macromolecular structures
    • Hendrickson, W. W. 1985. Stereochemically restrained refinement of macromolecular structures. Methods Enzymol. 115:252-270.
    • (1985) Methods Enzymol. , vol.115 , pp. 252-270
    • Hendrickson, W.W.1
  • 13
    • 84945096204 scopus 로고
    • Model bias in macromolecular crystallography
    • Hodel, A., S.-H. Kim, and A. T. Brünger. 1992. Model bias in macromolecular crystallography. Acta Crystallogr. A48:851-858.
    • (1992) Acta Crystallogr. , vol.A48 , pp. 851-858
    • Hodel, A.1    Kim, S.-H.2    Brünger, A.T.3
  • 14
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., J.-Y. Zou, S. W. Cowan, and M. Kjeldgaard. 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A47:110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 15
    • 0025943869 scopus 로고
    • Exploration of disorder in protein structures by x-ray restrained molecular dynamics
    • Kuriyan, J., K. Osapay, S. K. Burley, A. T. Brünger, and W. A. Hendrickson. 1991. Exploration of disorder in protein structures by x-ray restrained molecular dynamics. Proteins. 10:340-358.
    • (1991) Proteins , vol.10 , pp. 340-358
    • Kuriyan, J.1    Osapay, K.2    Burley, S.K.3    Brünger, A.T.4    Hendrickson, W.A.5
  • 16
    • 0032212015 scopus 로고    scopus 로고
    • Incorporation of prior phase information strengthens maximum-likelihood structure refinement
    • Pannu, N. S., G. N. Murshudov, E. J. Dodson, and R. J. Read. 1998. Incorporation of prior phase information strengthens maximum-likelihood structure refinement. Acta Crystallogr. D54:1285-1294.
    • (1998) Acta Crystallogr. , vol.D54 , pp. 1285-1294
    • Pannu, N.S.1    Murshudov, G.N.2    Dodson, E.J.3    Read, R.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.