Contains Carbon Carbohydrates Lipids Nucleic Acids Proteins.

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Presentation transcript:

Contains Carbon Carbohydrates Lipids Nucleic Acids Proteins

Contains Carbon, Hydrogen, and Oxygen Carbohydrates Lipids Nucleic Acids Proteins

Contains Carbon, Hydrogen, and Oxygen, Nitrogen Proteins

Contains Carbon, Hydrogen, and Oxygen, Nitrogen, Phosphorus Nucleic Acids

Carbohydrate Monosaccharide = monomer unit

Lipids Glycerol + fatty acid lipids + water Saturated -- only single bonds, maximum number of H atoms Unsaturated -- at least one C = C double bond lipid lipid Glycerol + fatty acid lipids + water

Nucleic acids Monomer—nucleotide Nucleotide = phosphate, pentose sugar, Nitrogenous base phosphodiester bond

Protein Monomer units are amino acids Amino Acids are identified by their different R Group

The primary structure of a protein is its unique sequence of amino acids. Lysozyme, an enzyme that attacks bacteria, consists on a polypeptide chain of 129 amino acids. The precise primary structure of a protein is determined by inherited genetic information. Fig. 5.18 Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings

Even a slight change in primary structure can affect a protein’s conformation and ability to function. In individuals with sickle cell disease, abnormal hemoglobins, oxygen-carrying proteins, develop because of a single amino acid substitution. These abnormal hemoglobins crystallize, deforming the red blood cells and leading to clogs in tiny blood vessels. Fig. 5.19 Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings

The secondary structure of a protein results from hydrogen bonds at regular intervals along the polypeptide backbone. Fig. 5.20 Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings

Tertiary structure is determined by a variety of interactions among R groups and between R groups and the polypeptide backbone. Fig. 5.22 Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings

Quarternary structure results from the aggregation of two or more polypeptide subunits. Collagen is a fibrous protein of three polypeptides that are supercoiled like a rope. This provides the structural strength for their role in connective tissue. Hemoglobin is a globular protein with two copies of two kinds of polypeptides. Fig. 5.23 Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings

A protein’s function depends on its specific conformation A functional protein consists of one or more polypeptides that have been precisely twisted, folded, and coiled into a unique shape. It is the order of amino acids that determines what the three-dimensional conformation will be. Fig. 5.17 Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings

Fig. 5.24 Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings

Enzymes Proteins that help speed up reactions

Enzymes LACTOSE LACTOSE glucose galactose lactase lactase lactase

Protein inhibitors Enzymes can have an allosteric inhibitor in which another molecule can turn the enzyme on or off by binding to it (make the “lock” work or not)

The main parts of the cell membrane

Phospholipids

Endo and Exocytosis