lecture 3: Macromolecules

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28 Terms

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Proteins structure

  • formed of one or more polypeptide chains

  • overlapping with itself

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polypeptides

  • made up of chains of amino acids

  • has a N-terminus where the protein/polypeptide starts and a C-terminus where it ends

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protein functions

  • Enzymes: catalyzes reactions

  • Structural: support, shape, and cytoskeleton

  • Motility: *cellular movement*, movement of organelles within the cell, and organismal movement through muscle contraction

  • Regulatory: control of other functions

  • Defence: antibodies

  • Communication

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Polymerization 

  • Protein synthesis

  • Making polymers from monomers via Ribosomes

  • Condensation and dehydration reactions loses H2O to form an amide/peptide bond

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Monomer

A subunit

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Polymer

The complex of subunits

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Monomeric Protein

Formed of just one polypeptide

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Multimeric Protein

More than one polypeptide

  • homomeric

  • heteromeric

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Homomeric polypeptide

Has either two alpha helix’s or two beta sheets

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Heteromeric

has both an alpha and a beta head

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Protein folding

Conformation of protein dependent in amino acids acid sequence

  • interactions between amino acids

  • covalent (disulfide)

  • Ionic

  • Hydrogen

  • Hydrophobic

  • Van der Waals

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Intramolecular

Within the same molecule

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Intermolecular

Between multiple molecules

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Levels of protein structure - Primary

  • The sequence of amino acids from N-terminus to C-terminus

  • determines protein folding

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Levels of protein structure - Secondary

  • alpha helix

  • beta sheets

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Levels of protein structure - Tertiary

  • three-dimensional folding

  • determined by interactions between amino acid chains

  • involves:

    • disulfide bonds

    • ionic bonds

    • hydrogen bonds

    • hydrophobic interactions

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Quaternary Structure

  • arrangement of multiple polypeptide chains

  • e.g. hemoglobin

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Amino acids

  • twenty different protein-forming sections

  • contains:

    • amino group

    • carboxyl group

    • central carbon

    • Side chain (R group)

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Nucleic acids

  • composed of nucleotides

    • bases

    • nucleosides

    • nucleotides

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Three types of RNA

  • tRNA

  • rRNA

  • mRNA

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Carbohydrates

  • made up of polysaccharides

    • the monomer unit is polysaccharides

    • d-glucose is the most common

    • used for both storage and structural

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Lipids

  • very hydrophobic, mostly non-polar

  • energy, structural, and functional

  • has 6 classes

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Classes of lipids

  1. Fatty acids

  2. Triacylglycerols

  3. Oleomargarine

  4. Phospholipids

  5. Glycolipids

  6. Steroids

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Fatty Acids

  • mainly building blocks for other classes

  • created by stepwise addition of two-carbon units

  • unsaturated fatty acids have bends/kinks

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Triacylglycerols

  • also known as triglycerides

  • storage/insulation

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Phospholipids

amphipathic lipid molecules

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glycolipids

  • lipids with carbohydrate groups

  • often involved in signalling/recognition

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Steroids

  • involved in membrane structures

  • signalling