320Fall09Lecture3 - BIO 320 Cell Biology, Fall `09 Dr....

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BIO 320 Cell Biology, Fall ‘09 Dr. Thomas Bushart Lecture 3
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Topics Protein folding and function Protein degradation I Proteasome I Ubiquitin tagging Misfolding and disease
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Self assembly Secondary tertiary folding can occur unaided I May require assistance from chaperones Individual subunits may interact in ways that lead to superstructures and highly ordered patterns I May need scaffolding or processing however
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Tomato bushy stint virus
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Subunit advantage Small amount of DNA can produce large structures Assembly and disassembly are controllable I Growth and shrinkage of cytoskeletal fibers Error correction I Badly made subunits simply won’t be used
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Protein function Proteins work by binding I Shape I Intermolecular bonding
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Protein binding
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Reactivity The arrangements of side chains may result in unexpected reactivities
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Proteins as enzymes Enzymes work by binding too I NOT like a glove Increase likelihood of the reaction I Bring reactants in close proximity I Alter electron distribution to favor reaction I Bind more favorably to the transition state
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Reaction complexes Most enzymes are extremely specific in activity Enzymatic pathways utilize many enzymes to take small steps towards a final product Increase efficiency via spatial association
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At a basic level, how would you modulate the activity of a protein?
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This note was uploaded on 09/15/2009 for the course BIO 320 taught by Professor Staff during the Fall '08 term at University of Texas at Austin.

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320Fall09Lecture3 - BIO 320 Cell Biology, Fall `09 Dr....

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