Term
| Different functional categories of proteins |
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Definition
structural catalysts movement transport defense hemostasis regulation lubricants |
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Term
| Example of structural proteins |
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Definition
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Term
| Examples of movement proteins |
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Definition
myosin actin troponin tropomyosin tubulin |
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Term
| Example of transport proteins |
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Definition
albumin hemoglobin transferrin (transport iron) ceruloplamsin (transport copper) |
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Term
| Examples of defense proteins |
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Definition
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Term
| Example of hemostasis proteins |
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Definition
fibrinogen factor X plasmin thrombin |
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Term
Example of regulation proteins |
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Definition
insulin thyrotropin PTH GF's |
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Term
Example of lubricant proteins |
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Definition
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Term
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Definition
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Term
| What is the only AA that does not have an asymmetric alpha carbon? |
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Definition
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Term
Configuration of amino acids in the body |
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Definition
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Term
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Definition
| made up of only AA, so upon hydrolysis, it yields a mix of AA's |
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Term
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Definition
made up of AA's plus other organic molecules/ions (aka cofactors) |
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Term
| Repeating backbone sequence of polypeptide |
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Definition
amine group alpha carbon carboxyl group |
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Term
| What groups project off the backbone of a polypeptide? |
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Definition
| R groups (can be a variety of function groups) |
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Term
| Define primary structure of protein |
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Definition
| sequence of AA's dictated by DNA |
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Term
| Define native confirmation/tertiary structure |
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Definition
| 3D shape the polypeptide takes when placed into its natural environment |
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Term
| Examples of common shapes seen in tertiary structure of protein |
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Definition
rods (ex: Type I, II, III collagen, keratin) sheets globule (ex: transport proteins, Ab's)
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Term
| How does the protein know how it should fold into its tertiary structure? |
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Definition
| AA sequence dictates folding |
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Term
| Major factors that dictate folding of polypeptide |
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Definition
IT DOESNT ALWAYS WORK OUT THAT WAY!!! |
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Term
| Define secondary structures |
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Definition
specfic folding of certain segments of polypeptide backbone into specific, well defined structures (so multiple secondary structures make up the tertiary structure) |
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Term
Most common secondary structures |
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Definition
alpha helix beta confirmation random coils |
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Term
| Most common secondary structure helix |
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Definition
alpha helix (3.613 helix) 3.6 AA's (interchain H bond between every fourth AA) for one turn, you should have 13 atoms between hydrogen bonds
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Term
| Why is an alpha helix the most stable structure |
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Definition
it allows for maximal interchain hydrogen bonding between carbonyl oxygen and amino group |
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Term
| What other helical structures would you see in a protein? |
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Definition
310 (tighter) 4.416 (looser) |
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Term
| How do you read the direction of the polypeptide when in beta confirmation |
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Definition
| amino end to carboxyl end |
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Term
| Structure of beta confirmation |
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Definition
zig zag structure R groups of AA's are projecting up in down in the plane carbonyl oxygen and H are projecting perpendicular (C comes toward me, H to the side)
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Term
Define quaternary structure |
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Definition
| how various subunits (polypeptides) interact with each other |
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Term
| Define the subunit of the quarternary structure |
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Definition
| polypeptide that interacts/"bonds" with another |
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Term
| Subunits of creatine kinase in the heart? in the muscle? |
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Definition
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Term
| When would we see increases in creatine kinase? |
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Definition
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Term
| Describe structure of beta pleted sheet |
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Definition
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Term
| Definition of Super secondary structure |
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Definition
| several secondary structures folding together; very discrete units of tertiary structure |
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Term
| Major bond that stabilizes all secondary structure |
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Definition
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Term
Types of interactions that stabilize the structure of a protein |
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Definition
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Term
| What different levels of protein structure are hydrophobic bonds involved in? |
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Definition
super secondary tertiary quarternary |
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Term
| Describe how an electrostatic/salt bond is formed |
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Definition
| acidic AA's form bridges with basic AA's |
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Term
| How is a disulfide bond formed |
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Definition
bonding of the thiol groups of two cysteine molecules |
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Term
| Ways to denature a protein |
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Definition
heating high urea concentration (break H bonds) anionic and cationic detergents (soaps) extreme pH's (change charge on AA) some organic solvents shaking/aeration
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Term
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Definition
loss of proteins native confirmation so it loses its unique tertiary structure and goes into a different structure WITHOUT breaking covalent bonds |
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Term
| What type of protein is it common to see disulfid bonds in? |
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Definition
| structural prteins like collagens, keratins |
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Term
| Effect of proline on alpha helix |
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Definition
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