Lecture9 - Lecture 9 1/28/09 Background reading: Garrett...

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Lecture 9 1/28/09 Renaturation of proteins Dialysis Primary structure determines tertiary structure Globular proteins Cytochrome c Myoglobin Background reading: Garrett and Grisham: Chapter 5: Pages 132 -134 Chapter 6: Pages 171 - 191
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Renaturation of proteins Key experiment was done by Anfinsen and colleagues in the early 1960s. Original protein Denatured protein Renatured protein The removal of a denaturing agent sometimes leads to the refolding of the protein to its native conformation Worked on ribonuclease – catalyzes the breakdown of RNA. . Small protein of 124 amino acids – for diagram see Figure 5.6, Page 109 in the Garrett book. Has 8 cysteines. In the native structure, disulfide linkages occur between the following cysteines: 26 and 84; 40 and 95; 58 and 110; 65 and 72.
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This treatment transformed the enzyme to a random coil structure which had no enzyme activity. Then removed the urea and mercaptoethanol by dialysis. Dialysis Use of a semipermeable membrane to separate low molecular weight components, such as salts and various reagents from high molecular weight components such as proteins. Dilute
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This note was uploaded on 02/21/2009 for the course BIS BIS102 taught by Professor Hilt during the Winter '08 term at UC Davis.

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Lecture9 - Lecture 9 1/28/09 Background reading: Garrett...

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