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Contains Carbon Carbohydrates Lipids Nucleic Acids Proteins.

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Presentation on theme: "Contains Carbon Carbohydrates Lipids Nucleic Acids Proteins."— Presentation transcript:

1 Contains Carbon Carbohydrates Lipids Nucleic Acids Proteins

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

3 Contains Carbon, Hydrogen, and Oxygen, Nitrogen
Proteins

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

5 Carbohydrate Monosaccharide = monomer unit

6 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

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

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

9 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

10 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

11 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

12 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

13 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

14 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

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

16 Enzymes Proteins that help speed up reactions

17 Enzymes LACTOSE LACTOSE glucose galactose lactase lactase lactase

18 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)

19 The main parts of the cell membrane

20 Phospholipids

21

22 Endo and Exocytosis

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