BIOLOGY 2B03 Lecture Notes - Lecture 2: Cysteine, Atp Hydrolysis, Ataxia
1 Sep 2020
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Document Summary
Most protein molecules fold rapidly into their native conformation. Molecules can assist incompletely folded proteins to fold properly using machinery within the cell = chaperones or chaperonin complexes. However, chaperones and chaperonin complexes approach this task in slightly different ways. If ultimately these proteins cannot be folded, aggregates can form = detrimental to the cell. Instead these proteins will be removed by the cell via degradation in the proteasome. Chaperones fall into 2 classes: the first class includes monomeric molecular chaperones and the second class includes the multimeric chaperonin complex. Assist in folding in similar way --> prevent inappropriate interactions/folding within the molecule or with other proteins, increasing the efficiency of protein folding. They are not directing folding in a particular way. These mechanisms are ubiquitous, meaning that they are seen in all organisms and in all subcellular compartments where protein folding occurs.
