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

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Presentation on theme: "MOLECULAR CHAPERONES The Department of Biochemistry of Medical Faculty Presents now Edited by Attila Sandor."— Presentation transcript:

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

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

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

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

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

9 (a)The folding of the unfolded protein (U) to the correct (C) form is favored thermodynamically. Chaperone is not necessary. (b)The folding of the unfolded protein (U) to the incorrect (I) form is favored thermodynamically. Chaperone is necessary. Role of chaperones in the thermodynamic point of view 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 Nucleoplasmins Chaperonins Heat shock proteins 70 ( Hsp70) Nucloplasmin NucleoplasminS chaperonin 60, groEL chaperonin 60, groEL chaperonin 10, groES (mitochondrial, bacterial) may use ATP Heat shock proteins 90 (Hsp90) Ellis R.J., Annu. Rev. Biochem., 1991

12 DNA + Histoneaggregate DNA+ Nucleoplasmin + HistoneNucleosoma (DNA + Histone) Nucleoplasmin Role of nucleoplasmines: assably of chromatin Author`s picture

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

14 Rubisco denaturated with guanine at +10 o C RUBISCO and the chaperonins Rubisco denaturated with guanine at +25 o C and chaperonin 60, chaperonin 10, ATP, Mg ++ were added When removing guanine very poor recovery 80% recovery Rubisco denaturated with guanine at +25 o C good 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 Attila Sandor c:\sandor\chaperon.ppt


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