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Biochem chapter 10
| Question | Answer |
|---|---|
| Amino Acids Contain | -NH3+ (amine) -COO (carboxylic) |
| What an alpha carbon | Where the two functional (amine and carboxylic) groups are combined |
| L AA | H3N+ on Left |
| D AA | H3N+ on Right |
| Non Polar Amino Acids | Glistening Albatrosses Value Learnable Interesting Pho, Mexican Prongs Try |
| mnemonic to memorize Non Polar Amino Acids | Glycine, Alanine, Valine, Leucine, Isoleucine, Phenylanine, Methionine, Proline, Tryptophan |
| Mnemonic to memorize Polar Amino Acids | Serious Thneeds Try Cyan Aspargus. Glutamine |
| Polar Amino Acids (neutral) | Serine, Threonine, Tyrosine, Cysteine, Aspargine, Glutamine |
| Polar Amino Acids (acidic) | Asparte, Glutamate (Ashy Gatorade) |
| Polar Amino Acids (Basic) | Histidine, Lysine, Agrine (He Lies Anally) |
| Whats a zwitterion | The ionic form of an AA existing no net charger, cancels eachother out |
| Isoelectric point (PI) | The pH at which an AA has a net charge of zero |
| Say the PI for Cystine is 5.1. What is the net charge of the AA at these volumes? pH 2.0 pH 5.1 pH 10.5 | 2.0- acidic. so +1 5.1- the same as PI. so 0 10.5- Basic. so -1 |
| Condensation | Removing OHs and Hs (building) |
| Hydrolysis | Adding OHs and Hs (Breaking) |
| When amino acids combine from ______ a _____ is formed | Condensation; Peptid bond |
| Primary structure | The order of the Amino Acids bonded by peptide bond, forming a polypeptide chain |
| Secondary structure | Where patterns are formed - alpha helix - beta pleated sheet |
| Tertiary structure | When the secondary structure (alpha+beta) fold in on themselves, so now they are interacting! - Creates a 3d shape - Globular |
| 3S Non polar interactions | Hydrophobic |
| 3S Polar interactions | Hydrophilic |
| Salt bridges? | Where the NH3+ and COO form |
| Disulfide Bonds | Covalent bonds formed between 2 cystonines (they are SH groups) |
| Quaternary Structures | Globs on Globs |
| Denaturation | A process that disrupts the stabilizing attractive forces in the 2nd, 3rd, or 4th structure |
| Is the primary structure changed in denaturation? | NO. |
| What bonds are affected during denaturation? | 1. H bonds 2. Salt bridges 3. Disulfide Bonds |
| 2 Examples of denaturation | 1. Hair straightening, Hair perms 2. Egg whites turning white -> clear when heated |
| What are enzymes? | Catalysts! They accelerate metabolism |
| During what structure do enzymes happen? | 3rd |
| What are active sites? | The area of the enzyme involved in the catalysis of chemical reactions |
| What is a substrate? | The reactant in a chemical reaction catalyzed by an enzyme |
| Cofactors and Coenzymes | 2 non protein helpers |
| What is the initial interaction between an enzyme and a substrate called? | The Enzyme Substrate Complex [ES] |
| When does the ES formation occur? | Before catalysis begins |
| Lock and key model | Perfect fit no change |
| Induced fit model | The enzyme changes itself to fit with the substrate |
| An enzyme _____ the activation energy of a reaction, which _____ the rate of a reaction. Enzymes accomplish this by first forming ______ | 1. Lowers 2. Increases 3. Enzyme Substrate |
| The enzyme substrate complex reacts faster than the reactant on its own due to 3 factors FIRST | PROXIMITY Once glucose + ATP come together, in the enzyme, it makes it easier to find eachother |
| The enzyme substrate complex reacts faster than the reactant on its own due to 3 factors SECOND | ORIENTATION enzyme brings these molecules together in a certain way that makes these reactions happen |
| The enzyme substrate complex reacts faster than the reactant on its own due to 3 factors THIRD | BOND STRENGTH The enzymes often have weakened substrate. This now breaks faster! |
| Do products fit into the active site once the reaction occurs? | No :( |
| Measuring how fast an enzymatic reaction occurs is a measure of an enzyme's | ACTIVITY |
| 2 Environmental impacts on enzyme activity | 1. pH change (ATT Forces are broken) 2. Enzymes only work at 37 C |
| Higher temp in enzymes | Can lose ATT forces DENATURED |
| Lower temp in enzymes | Lack of energy to get over the activation energy barrier |
| Want to slow an enzyme? | STORE AT LOW TEMP |
| Want to KILL an enzyme???? | BOIL WATER |
| Inhibitors | A molecule that causes an enzyme's catalytic activity to DECREASE |
| Reversible Inhibitors | Temporary!! Can be COMPETITIVE or NON COMPETITVE |
| Competitive Inhibitors | Molecules that compete with the substrate for the activity side |
| Non Competitve Inhibitors | Don't look like the susbtrate SO.... NON comp for the enzyme's activity site |
| Where do Non Competitve Inhibitors bind? | Elsewhere, causing the enzyme's shape to distort It can't function anymore :( |
| Where do irreversible inhibitors bind? | They covalently bind to the active site CAN NOTTTT BE REVERSED |
| What type of interaction holds alpha helicase and beta pleated sheets together? | H-bonds between backbone O and the NH of an amino acid further along the chain |
| Cd ions are inhibitors of hexokinase. Increasing the concentration of glucose or ATP, the substrate of hexokinase, or MG2+, the cofactor of hexokinase, does not change the rate of the CD inhibited rxn. What does this indicate about the effect of CD | It is a non competitive inhibitor of hexokinase |
| Protonated | Protonated means a molecule has gained a proton (\(H^{+}\)), making it more positively charged or less negatively charged |
| Deprotonated | deprotonated means it has lost a proton, making it more negatively charged or less positively charged |
| If the acid group has a pKa of 2.8, and the amino group has a pKa of 9.8, what is the charge of this peptide at the following PH In the stomach- 2.0 pH | PROTONATED ph<pKa POSITIVE Charge |
| If the acid group has a pKa of 2.8, and the amino group has a pKa of 9.8, what is the charge of this peptide at the following PH In a solution of 10 pH | DEPROTONATED pH>pKa NEGATIVE Charge |
| If the acid group has a pKa of 2.8, and the amino group has a pKa of 9.8, what is the charge of this peptide at the following PH In the small intestine of 7.4 pH | PROTONATED pH>pKa NEGATIVE CHARGED |
Created by:
liladdoyle