Happy Monday! 9/16/2013 PQ & Journal—7.5 & 7.6 Test Wednesday, let’s boogy!

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4 Macromolecules in all living organisms:

Table 3.1

Polymers are formed in condensation reactions.

Figure 3.4 Condensation of Polymers : Water is removed; Cov bond forms b/w monomers

Figure 3.4 Hydrolysis of Polymers– water is added; cov bond b/w monomers is broken

6 Functions of proteins: (IB)

Proteins are made from 20 different amino acids (monomeric units)

The composition of a protein:

7.5.2 Outline the difference between fibrous proteins & globular proteins, with reference to two examples of each protein type. FibrousGlobular Shape Solubility Main level of organization Function Examples

Parts of an amino acid Amino acids have

These hydrophylic amino acids attract ions of opposite charges. Table 3.2 (Part 1): HYDROPHILIC AMINO ACIDS

Hydrophylic amino acids with polar but uncharged side chains form hydrogen bonds Table 3.2 (Part 2): POLAR, UNCHARGED (HYDROPHILIC)

Table 3.2 (Part 3): NONPOLAR, HYDROPHOBIC Hydrophobic amino acids

Table 3.2 (Part 4): WEIRDOS

Figure 3.5 Disulfide Bridge FORMATION BETWEEN TWO CYSTEINES (covalent bond)

Figure 3.6 Formation of Peptide Bonds: amino of 1, carboxyl of another  peptide bond (condens.) The peptide bond is inflexible—no rotation is possible.

Primary Structure: Figure 3.7 The Four Levels of Protein Structure Amino acid monomersPeptide bond

Secondary structure: α helix— β pleated sheet—

Figure 3.7 The Four Levels of Protein Structure Secondary Structure:  Helix Hydrogen bond

Figure 3.7 The Four Levels of Protein Structure  Pleated sheet Secondary Structure: Hydrogen bond

Tertiary structure:

Figure 3.7 The Four Levels of Protein Structure Tertiary Structure  Pleated sheet  Helix Hydrogen bond Disulfide bridge

Quaternary structure results from the interaction of subunits by

Figure 3.7 The Four Levels of Protein Structure Quaternary Structure:

Figure 3.9 Quaternary Structure of a Protein

Figure 3.10 Noncovalent Interactions between Proteins and Other Molecules Ionic bonds b/w charged R groups 2 nonpolar groups interact hydrophobically H bonds form b/w 2 polar groups

Figure 3.11 Denaturation Is the Loss of Tertiary Protein Structure and Function Destroys its biological functions Renaturation: sometimes possible, but usually not

6 Energy, Enzymes, and Metabolism Alcohol dehydrogenase: catalyst for breakdown of alcohol

Catalysts speed up the rate of a reaction.

Activation Energy

Enzyme-Catalyzed Reactions

Figure 6.9 Enzyme and Substrate

Figure 6.10 Enzymes Lower the Energy Barrier

Figure 6.12 Some Enzymes Change Shape When Substrate Binds to Them: INDUCED FIT

Some enzymes require “partners”: Prosthetic groups: Cofactors: Coenzymes:

Figure 6.14 Catalyzed Reactions Reach a Maximum Rate

7.6.1 State that metabolic pathways consist of enzyme-catalysed reactions in: Chemical rxns usually multiple steps Each step has own enzyme Chains (glycolysis) Cycles (Krebs, Calvin Cycles)

Figure 6.17 Reversible Inhibition – inhibitor & substrate compete for active site

Figure 6.17 Reversible Inhibition– inhibitor binds to alternative site (not active site) & changes shape of active site Online Animated Tutorial

Figure 6.18 Allosteric Regulation of Enzymes INACTIVE FORMACTIVE FORM Inhibitor site Active site Activator site Catalytic subunit Regulatory subunits The enzyme switches back and forth between the two forms. They are in equilibrium. Online Animated Tutorial

Figure 6.18 Allosteric Regulation of Enzymes INACTIVE FORM Allosteric inhibitor Binding of an inhibitor makes it less likely that the active form will occur.