BIOC 192 - Module 1 (Protein structure and function)

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Last updated 7:41 AM on 7/20/26
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23 Terms

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Central dogma

This explains how genetic information flows across a cell. From DNA, to RNA and finally to proteins.

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ATP

energy currency of the cell

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What are the 4 groups attached to the central alpha carbon of an amino acid?

Amino group, acid group, hydrogen and R group

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Which amino acid is the only exception to having a chiral center?

Glycine (its R-group is just a Hydrogen atom, meaning the central carbon is not chiral).

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How is a peptide bond formed, and what are its key structural characteristics?

Formed via a condensation/dehydration reaction between the alpha-carboxyl group of one amino acid and the alpha-amino group of the next. Characteristics: It has partial double-bond character due to resonance, making it planar and rigid (restricting rotation around the C-N bond).

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How many different amino acids are there?

20

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Enzymes which break down proteins

Proteases

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Protein which breaks starch down into sugars

Amylase

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Enzyme which helps metabolise alcohol

Alcohol dehydrogenase

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Hormone in cell signalling to take up glucose

Insulin

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Protein which binds oxygen in the lungs and carries it in the blood to tissues for use in metabolism

Hemoglobin

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Membrane protein which generates ATP for use in cellular functions

ATP synthase

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Protein for DNA replication that binds to one strand of DNA and adds the complementary strand to it

DNA polymerase

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Protein that creates a single strand of RNA that is complementary to one of the strands of duplex DNA

RNA polymerase

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What is the main experimental technique used to determine protein structure?

Protein crystallography

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Imino acid which does not have a protonated side chain

Proline (P), Pro

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4 classifications of amino acids

Non-polar side chains, Polar side chains uncharged, Polar side chains charged acidic and basic

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Two types of amino acid abbreviations

3 letter and 1 letter

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pKa value

The pH at which the amino acid or protein group is 50% ionised

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Isoelectric point (pI)

The pH at which the net chrage of an amino acid or protein is zero

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When an amino acid is modified after it has been added to a protein

Post translational modification

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Bond that forms when two cysteines for a covalent bond

Disulfide bond

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