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GOB Chemistry: Lipids, Amino Acids, Proteins, and Enzymes

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Terms in this set (22)

  • Types of lipids

    Lipids include fatty acids, waxes, triacylglycerols (oils and fats), phospholipids, and steroids.

  • Fatty acids classification

    Fatty acids are classified as saturated, monounsaturated, or polyunsaturated based on the number of double bonds.

  • Composition of triacylglycerols

    Triacylglycerols are composed of three fatty acids esterified to a glycerol backbone.

  • Chemical properties of triacylglycerols

    Triacylglycerols undergo hydrogenation, hydrolysis, and saponification.

  • Hydrogenation of triacylglycerols

    Hydrogenation adds hydrogen to unsaturated bonds, converting oils to fats and increasing saturation.

  • Hydrolysis of triacylglycerols

    Hydrolysis breaks triacylglycerols into glycerol and free fatty acids using water and enzymes or acid/base.

  • Saponification

    Saponification is the base-catalyzed hydrolysis of triacylglycerols producing glycerol and soap (salts of fatty acids).

  • Phospholipids structure

    Phospholipids have two fatty acids, a glycerol backbone, and a phosphate group, making them amphipathic.

  • Steroids composition and uses

    Steroids have a four-ring structure and are used as hormones and membrane components.

  • Cell membrane and transport

    Phospholipids form bilayers in membranes, controlling transport of substances across the membrane.

  • Amino acid classification by polarity

    Amino acids are classified as polar or non-polar based on side chain properties.

  • Amino acid classification by charge

    Amino acids are classified as acidic or basic depending on the charge of their side chains at physiological pH.

  • Primary structure of proteins

    The primary structure is the linear sequence of amino acids in a polypeptide chain.

  • Secondary protein structures

    Secondary structures include alpha helices and beta sheets stabilized by hydrogen bonds.

  • Tertiary and quaternary protein structures

    Tertiary structure is the 3D folding of a single polypeptide; quaternary is the assembly of multiple polypeptides.

  • Attractive forces in protein structures

    Forces include hydrogen bonds, ionic bonds, hydrophobic interactions, and disulfide bridges.

  • Protein denaturation

    Denaturation disrupts protein structure by heat, pH changes, chemicals, or mechanical forces, affecting function.

  • Enzyme classification

    Enzymes are classified by the type of reaction they catalyze, such as oxidoreductases, transferases, hydrolases, etc.

  • Lock and key model of enzyme action

    The enzyme's active site has a specific shape that fits the substrate exactly like a key in a lock.

  • Induced fit model of enzyme action

    The enzyme changes shape upon substrate binding to better fit and catalyze the reaction.

  • Factors affecting enzyme activity

    Enzyme activity is affected by temperature, pH, substrate concentration, and inhibitors.

  • Enzyme inhibition types

    Inhibitors can be competitive (bind active site) or non-competitive (bind elsewhere).