Study of tyrosine-containing mutants of ribosomal protein L7/L12 from Escherichia coli

Biophysical Chemistry

Volumn 62, Issue 1-3, 1996, Pages 39-45

  Todorova, Roumiana T ^a   Rogov, Vladimir V ^b   Vasilenko, Kostia S ^b   Permyakov, Eugene A ^c  

^a INSTITUTE OF BIOPHYSICS AND BIOMEDICAL ENGINEERING   (Bulgaria)

^b INSTITUTE OF PROTEIN RESEARCH   (Russian Federation)

^c INSTITUTE OF THEORETICAL AND EXPERIMENTAL BIOPHYSICS   (Russian Federation)

Author keywords

Circular dichroism; Fluorescent spectroscopy; Microcalorimetry; Mutant proteins L7 L12; pH titration curves; Thermostability

Indexed keywords

MUTANT PROTEIN; RIBOSOME PROTEIN;

ARTICLE; CIRCULAR DICHROISM; ESCHERICHIA COLI; FLUORESCENCE SPECTROSCOPY; GENE CONSTRUCT; GENE EXPRESSION; GENE TRANSFER; MICROCALORIMETRY; MUTANT; PH; PRIORITY JOURNAL; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; TECHNIQUE; TEMPERATURE;

BACTERIAL PROTEINS; CALORIMETRY, DIFFERENTIAL SCANNING; CIRCULAR DICHROISM; DIALYSIS; ESCHERICHIA COLI; HYDROGEN-ION CONCENTRATION; MUTATION; PHENYLALANINE; PROTEIN DENATURATION; RIBOSOMAL PROTEINS; SPECTROPHOTOMETRY, ULTRAVIOLET; TEMPERATURE; TYROSINE;

ESCHERICHIA COLI;

EID: 0030606326     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(96)02176-X     Document Type: Article

References (21)

1. [1] W. Moller, A. Groene, C. Terhorst and R. Amons, Eur. J. Biochem., 25 (1972) 5-12.
2. [2] K.-P. Wong and H.H. Paradies, Biochem. Biophys. Res. Commun., 61 (1974) 178-184.
3. [3] A.T. Gudkov, J. Behlke, N.N. Vtiurin and V.I. Lim, FEBS Lett., 82 (1977) 125-129.
4. [4] C.A. Luer and K.P. Wong, Biochemistry. 18 (1979) 2019-2027.
5. [5] A. Liljas, Prog. Biophys. Mol. Biol., 40 (1982) 161-228.
6. [6] C.P. Terhorst, B. Wittman-Liebold and W. Moller, Eur. J. Biochem., 25 (1972) 13-19.
7. [7] M. Leijonmarck, S. Ericsson, and A. Liljas, Nature, 286 (1980) 824-826.
8. [8] M. Leijonmarck, and A. Liljas, J. Mol. Biol., 195 (1987) 555-580.
9. [9] A.J. Van Agthoven, J.A. Maassen, P. Schrier and W. Moller, Biochem. Biophys. Res. Commun., 64 (1975) 1184-1191.
10. [10] V.N. Bushuev, A.T. Gudkov, A. Liljas and N.F. Sepetov, J. Biol. Chem. 264 (1989) 4498-4505.
11. [11] V.E. Koteliansky, S.P. Domogatsky and A.T. Gudkov, Eur. J. Biochem., 90 (1978) 319-323.
12. [12] A.T. Gudkov and J. Behlke, Eur. J. Biochem., 90 (1978) 309-312.
13. [13] R.T. Todorova, Bioorganicheskaya Khimia. 19 (1993) 286-292.
14. [14] E.A. Permyakov, E.A. Burstein, Y. Sawada and Y. Yamazaki, Biochim. Biophys. Acta, 491 (1977) 149-154.
15. [15] P.L. Privalov and S.A. Potekhin, Methods in Enzymology, 131 (1986) 4-51.
16. [16] P.L. Privalov, Pure Appl. Chem., 52 (1980) 479-497.
17. [17] S.A. Potekhin and P.L. Privalov, J. Mol. Biol., 159 (1982) 519-535.
18. [18] A. Darbre (Ed.), Practical Protein Chemistry - A Handbook, Wiley, Chichester, 1986.
19. [19] A.C. Luer and K.-P. Wong, Biochemistry, 19 (1980) 176-183.
20. [20] A.T. Gudkov, N.N. Khechinashvili and V.N. Bushuev, Eur. J. Biochem., 90 (1978) 313-318.
21. [21] P.L. Privalov and N.N.J. Khechinashvili, Mol. Biol., 86 (1974) 665-684.