GENE 500 Lecture Notes - Lecture 3: Alternative Splicing, Protein Folding, Intron
Document Summary
Molecular chaperones, which bind to a short segment of a protein substrate and stabilize unfolded or partly folded proteins, thereby preventing these proteins from aggregating and being degraded. Hsp70 and its homologs are the major chaperones in all organisms that use an atp-dependent cycle to fold their substrates. Chaperonins, which form folding chambers into which all or part of an unfolded protein can be sequestered, giving it time and an appropriate environment to fold properly. Even though protein folding is thermodynamically stable, kinetically, its not so good hence, folding is assisted by proteins to speed up the process. It is because they are very difficult to fold correctly. This is due to alter(cid:374)ative splici(cid:374)g i(cid:374) eukaryotes (cid:894)so(cid:373)e i(cid:374)tro(cid:374)s are i(cid:374)cludes, so(cid:373)e are re(cid:373)oved, etc (cid:895) Tissue specific adaptation: if you sequence a protein in tissue, it may have different alternative splicing that if you sequenced it in another tissue. If protein misfolds, it gets ubiquitinated (gets tagged)
