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MOLECULAR CHAPERONES

The Department of Biochemistry of Medical Faculty. Presents now. MOLECULAR CHAPERONES. Edited by Attila Sandor. one dimensional information. three dimensional information. L. Fig.3-16, p.89. The model proteins for classic study of developing the

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MOLECULAR CHAPERONES

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  1. The Department of Biochemistry of Medical Faculty Presents now MOLECULAR CHAPERONES Edited by Attila Sandor

  2. one dimensional information three dimensional information L. Fig.3-16, p.89

  3. The model proteins for classic study of developing the three dimensional structure, that for folding. (Anfinsen) Str., Fig. 7.1, p.172

  4. Str. Fig. 3.53, p. 65

  5. Scrambled Str. Fig. 3.54, p. 66

  6. The three dimensional structure is dictated entirely by the amino acid sequence Str., Fig1.6 p.7

  7. Free energy L.Fig.4-29,p. 149

  8. Str. Fig. 3.57, p. 6+8

  9. Role of chaperones in the thermodynamic point of view • The folding of the unfolded protein (U) to the correct (C) form is favored thermodynamically. Chaperone is not necessary. • The folding of the unfolded protein (U) to the incorrect (I) form is favored thermodynamically. Chaperone is necessary. Ellis R.J., Annu. Rev. Biochem., 1991

  10. The idea of molecular chaperones Named after the human chaperone: “usually an elderly woman who accompanies a young unmarried lady to prevent not proper interactions with other people. Molecular chaperones: proteins assisting folding of nascent polypeptides, by preventing wrong folding. Molecular chaperones catalyze the formation of correctly folded, functionally active, native proteins, but they are not part of the product. Expression of many chaperon is induced by stress, such as by heat, because during heat-stress the probability of wrong folding is higher, therefore cells need more protection. These chaperons are called heat shock proteins (HSP’s). Author`s slide

  11. Representative members of the Chaperone family Heat shock proteins 70 ( Hsp70) Nucleoplasmins Nucloplasmin NucleoplasminS Chaperonins Heat shock proteins 90 (Hsp90) chaperonin 60, groEL chaperonin 60, groELchaperonin 10, groES (mitochondrial, bacterial) may use ATP Ellis R.J., Annu. Rev. Biochem., 1991

  12. Role of nucleoplasmines: assably of chromatin DNA + Histone aggregate DNA+ Nucleoplasmin + Histone Nucleosoma (DNA + Histone) Nucleoplasmin Author`s picture

  13. Representative members of the Chaperone family Heat shock proteins 70 ( Hsp70) Nucleoplasmins Nucloplasmin NucleoplasminS Chaperonins Heat shock proteins 90 (Hsp90) chaperonin 60, groEL chaperonin 60, groELchaperonin 10, groES (mitochondrial, bacterial) may use ATP Ellis R.J., Annu. Rev. Biochem., 1991

  14. RUBISCO and the chaperonins When removing guanine very poor recovery Rubisco denaturated with guanine at +25o C good recovery Rubisco denaturated with guanine at +10o C Rubisco denaturated with guanine at +25o Cand chaperonin 60, chaperonin 10, ATP, Mg++ were added 80% recovery Rubisco: ribulose 1,5-bisphosphate carboxylase-oxygenase Author`s slide

  15. L.Fig.41-31, p.152

  16. THANK YOU FOR YOUR ATTENTION The honored audience has the opportunity now to download the pictures of this lecture c:\sandor\chaperon.ppt Attila Sandor

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