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Volumn 4, Issue SUPPL., 1997, Pages 862-865

X-ray crystallography and NMR reveal complementary views of structure and dynamics

(1)  Brünger, Axel T a  

a NONE

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL STRUCTURE; MACROMOLECULE; MOLECULAR DYNAMICS; MOLECULAR WEIGHT; NUCLEAR MAGNETIC RESONANCE; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; SHORT SURVEY; X RAY CRYSTALLOGRAPHY;

EID: 0030791762     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Short Survey
Times cited : (85)

References (15)
  • 1
    • 0018793861 scopus 로고
    • Temperature-dependent X-ray diffraction as a probe of protein structural dynamics
    • Frauenfelder, H., Petsko, G.A. & Tsernoglu, D. Temperature-dependent X-ray diffraction as a probe of protein structural dynamics. Nature 280, 558-563 (1979).
    • (1979) Nature , vol.280 , pp. 558-563
    • Frauenfelder, H.1    Petsko, G.A.2    Tsernoglu, D.3
  • 2
    • 0020170342 scopus 로고
    • Conformational substates in a protein: Structure and dynamics of metmyoglobin at 80K
    • Hartmann, H. et al. Conformational substates in a protein: structure and dynamics of metmyoglobin at 80K. Proc. Natl. Acad. Sci. USA 79, 4967-4971 (1982).
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 4967-4971
    • Hartmann, H.1
  • 3
  • 5
    • 0000397184 scopus 로고
    • Protein structure by solid-state NMR
    • Cross, T.A. & Opella, S.J. Protein structure by solid-state NMR. J. Am. Chem. Soc. 105, 306-308 (1983).
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 306-308
    • Cross, T.A.1    Opella, S.J.2
  • 7
    • 0001204409 scopus 로고
    • X-ray Laue diffraction from protein crystals
    • Moffat, K., Szebenyi, D. & Bilderback, D. X-ray Laue diffraction from protein crystals. Science 223, 1423-1425 (1984).
    • (1984) Science , vol.223 , pp. 1423-1425
    • Moffat, K.1    Szebenyi, D.2    Bilderback, D.3
  • 8
    • 0031569799 scopus 로고    scopus 로고
    • The solution structure of serine protease PB92 from Bacillus alcalophilus presents a rigid fold with a flexible substrate-binding site
    • Martin, J.R. et al. The solution structure of serine protease PB92 from Bacillus alcalophilus presents a rigid fold with a flexible substrate-binding site. Structure 5, 521-532 (1997).
    • (1997) Structure , vol.5 , pp. 521-532
    • Martin, J.R.1
  • 9
    • 0031019983 scopus 로고    scopus 로고
    • Solution structure of the 30 kDa N-terminal domain of Enzyme I of the Escherichia coli phosphoenolpyruvate: Sugar phosphotransferase system by multidimensional NMR
    • Garrett, D.S. et al. Solution structure of the 30 kDa N-terminal domain of Enzyme I of the Escherichia coli phosphoenolpyruvate: Sugar phosphotransferase system by multidimensional NMR. Biochemistry 36, 2517-2530 (1997).
    • (1997) Biochemistry , vol.36 , pp. 2517-2530
    • Garrett, D.S.1
  • 10
    • 0029934934 scopus 로고    scopus 로고
    • 2H-decoupling
    • 2H-decoupling. J. Am. Chem. Soc. 118, 6570-6579 (1996).
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 6570-6579
    • Shan, X.1
  • 13
    • 5244224827 scopus 로고    scopus 로고
    • 1 an inhibitor of programmed cell death
    • 1 an inhibitor of programmed cell death. Science 381, 335-341 (1996).
    • (1996) Science , vol.381 , pp. 335-341
    • Muchmore, S.W.1
  • 14
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance in macromolecules. 1. Theory and range of validity
    • Lipari, G. & Szabo, A. Model-free approach to the interpretation of nuclear magnetic resonance in macromolecules. 1. Theory and range of validity. J. Am. Chem. Soc. 104, 4545-4559 (1982).
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4545-4559
    • Lipari, G.1    Szabo, A.2
  • 15
    • 0028019827 scopus 로고
    • Multidimensional nuclear magnetic resonance methods for protein studies
    • Bax, A. Multidimensional nuclear magnetic resonance methods for protein studies. Curr. Opin. Struct Biol. 4, 738-744 (1994).
    • (1994) Curr. Opin. Struct Biol. , vol.4 , pp. 738-744
    • Bax, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.