BCH 261 Lecture 10: Biochem Notes 10
16 Feb 2017
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It is mathematically impossible for protein folding to occur by randomly trying every (cid:272)o(cid:374)for(cid:373)atio(cid:374) u(cid:374)til the lo(cid:449)est e(cid:374)erg(cid:455) o(cid:374)e is fou(cid:374)d (cid:894)le(cid:448)i(cid:374)thal"s parado(cid:454)(cid:895) Search for the minimum is not random because the direction toward the native structure is thermodynamically most favorable. Energy landscape of protein folding -collapsed structures give rise to molten globules partially formed domains and motifs. Molecular chaperones interact with unfolded, improperly folded or partially folded proteins to facilitate folding or correct misfolding. Hsp proteins are conserved from bacteria to humans. Hsp proteins bind to regions of unfolded proteins. For example, after heat shock (thus the name), many proteins may become partially unfolded. Hsp recognizes these areas and binds to it. This prevents aggregation and helps proteins to refold properly. Sequesters a portion of the unfolded protein into its lumen to create a microenvironment which is conducive to proper folding. Amyloidosis: diseases caused when normally soluble proteins become unfolded, secreted from cells and forms insoluble protein structures.
