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Polymer
- •made of amino acid subunits (monomers)
- Book def is Any long molecule composed of small repeating units bonded together.
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Amino acid
A small organic molecule with a central carbon atom bonded to an amino group, a carboxyl group, a hydrogen atom and a side group. Proteins are polymers of 20 common amino acids. (side chain is what differs between types of amino acid) 
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Peptide bond
covalent bond between carboxyl group of one amino acid and the amino group of the amino acid next to it. (Covalent Bond)
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4 basic levels of organization of protein structures.
- Primary
- Secondary
- Tertiary
- Quaternary
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Primary Structure
sequence of amino acids (order matters)!!
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What if primary structure changes?
Each amino side chain has specific properties. The change of a single amino acid would change the function. Example is sickle cell disease.
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Secondary Structure
- results from hydrogen bonding between the carboxyl oxygen of one amino acid and the amino hydrogen of another. This is where the structure starts to becomes more 3-d like.
- Alpha helix is spirally Beta sheets are more straight.
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Alpha Helix / Beta sheets
- Proteins can have these multiple secondary structures.
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Tertiary Structure
interactions involving amino acid side chains. Hydrogen bonds / hydrophobic interactions. Hydrophobic parts will start to fold inside cause fuck that water.
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Quaternary structure
2 or more protein subunits will form a single functional protein.
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Structure summary
Primary, secondary, tertiary, Quaternary (happens all at once.)
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Molecular chaperones
Proteins that help other proteins fold
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Denatured
Not functioning
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Will proteins function if they are not folded?
No. Proper folding is required for functioning
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Enzymes
- Most proteins function as enzymes.
- They start chemical reactions, lower activation energy and are not consumed in the reaction.
- without enzyme
- with enzyme
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Temperature affects on enzyme function
- movement of substrates and enzyme
- enzyme shape
- Certain types of enzymes do better in specific temperatures.
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pH affects on enzyme function
- enzyme shape
- ideal temp and pH depends on environment of organism.
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Substrate
They are reactants that bind to active site of enzyme. enzyme binds only specific substrates.. not just to anything.
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Steps of enzymatic catalysis
- 1. reactants bind to the active site
- 2.interactions between the substrate and active site lower the activation energy.
- 3. Reaction products are released from the enzyme.
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Coenzymes / cofactors
additional factors required for normal enzyme function. (such as vitamins and minerals.)
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Competitive inhibition
- molecules similar in size and shape to the substrate will compete with the substrate for active site binding. This is a way to turn unneeded enzymes off "binds and blocks"
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Allosteric Regulation
- Molecule causes a change in enzyme shape by binding to the enzyme at a location other than the active site. closes enzyme active site, but can be reopened by other regulatory molecules.
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Biochemical Pathway
- Series of enzymatic reactions
- Product of reaction one becomes substrate of reaction two...
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Feedback inhibition
- a regulation method for biochemical pathways.
- If final product is abundant they don't waste energy by making more. Final product will bind to first enzyme to shut down chain. Can be restarted if more product is needed.
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