33917737
Description
Flashcards by Amy Bennett, updated more than 1 year ago
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Created by Amy Bennett
almost 3 years ago
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| Question | Answer |
| Monomer and Polymer of proteins? | M: Amino Acid P: Polypeptide |
| Monomer and Polymer of Nucleic acids? | M: Nucleotide P: DNA strand |
| Monomer and Polymer of Sugars? | M: Monosaccharide P: Starch |
| Monomer and Polymer of Lipids? | M: Fatty acid P: Triglyceride |
| 3 Ways to increase reaction rate | 1. Increase temp – decreased stability 2. Increase reactant concentration 3. Lower activation energy needed - Enzymes |
| Endergonic reaction? | Requires energy |
| Exergonic reaction? | Releases energy |
| What is a central dogma? | An explanation of the flow of genetic information within a biological system |
| What is a covalent bond? | Electron sharing |
| What is an ionic bond? | Electrons of one atom are transferred permanently to another atom - Salt bridges |
| pH and pOH equation is? | pH + pOH = 14 |
| Equation for determining pH | pH = - log10 [H+] |
| What is a buffer? | A substance that allows a solution that remain at a constant pH |
| 4 Functions of proteins and the products used to carry out their function | 1. Catalyse - DNA polymerase 2. Transport - hemoglobin 3. Structure - Collegen & keratin 4. Movement - Actin & myosin |
| How does the ionisation of amino acids change? | By changing the pH |
| Amino acids at a low pH exist as? | Cations (+ive charge) |
| Amino acids at a high pH exist as? | Anions (-ive charge) |
| Cations are either a. Pronated or b. de-pronated | Pronated - at carboxyl and amine groups |
| What is a Conjugated Protein? | A protein that functions in interaction with other (non-polypeptide) chemical groups |
| List 3 examples of a Conjugated Protein | Lipoproteins (lipid), Glycoproteins (carbs), Phosphoproteins (phosphate) or Hemoprotein (hemoglobin) |
| What is a Hydrogen bond? | Interaction of N-H and C-O between the H and O. |
| What is Van der Waals forces? | Weak attraction between atoms |
| Primary structure of proteins? | Peptide bonds |
| What are peptide bonds? | Amide bond that forms when the COO− group reacts with the NH3+ group of the next amino acid. |
| Name of peptide linking a. 2 amino acids b. 3 amino acids c. 4 amino acids | a. dipeptides b. tripeptides c. tetrapeptides |
| When adding 2 amino acids together they are joined by a peptide bond. How do you create this bond using chemical symbols? | Add amino acids together and replace 2 H and 1 O with a line. |
| How to name peptides | Add ly to the ends of all amino acids except those in the C-terminus |
| what are the 2 secondary structure of proteins? | 1. ? helix (alpha) 2. β pleated sheets (beta) |
| How are ? helix structures formed? Hint: types of bonds and numbers | H-bonds between O2 of the C==O groups and the H of N—H groups of the amide bonds in the next turn of the α helix. Formed between molecule n and molecule n + 4 |
| How are β pleated sheets formed? | H-bonds between carbonyl O2 atoms and H atoms in the amide groups |
| What is a β turn? (in relation β pleated sheets) | 180° turn When β sheets change direction |
| Tertiary structure of proteins. What are the 2 major classes? | 1. Fibrous 2. Globular (water soluable) |
| What does the Tertiary structure of proteins consist of? | Bonds between amino acid side chains. |
| Quaternary structure of proteins is? | The assembly of individual polypeptides into a larger functional cluster |
| What is a Ligand? | A molecule that binds to a protein |
| 2 types of binding specificity | 1. Lock and key model 2. induced fit model |
| Label the type of binding specificity and explain each | a. Lock and key model: ligand and binding site complementary b. Induced fit model: Ligands binds and cause structural change to binding site |
| The rate of enzymatic reactions are affected by? (4) | Types of Enzyme, substate, effector & temperature |
| Kinetic Parameters: What is Km and Vmax | Km = concentration of substrate that permits the enzyme to achieve half Vmax. Vmax = rate of reaction when enzyme is saturated with substrate is the maximum rate of reaction |
| Name, function & formula of graph shown | Name: Lineweaver-Burke plot Function: Used to calculate Vmax |
| Using this formula and and the Lineweaver-Burke plot identify what each colour represents | Green – y axis Red – x axis Blue – x, y intercept Purple – Slope of line |
| What is an enzyme inhibitor? | Compounds that decrease an enzyme’s activity |
| What is an Irreversible enzyme inhibitors (inactivators)? | 1 inhibitor molecules can permanently shut off 1 enzyme molecule |
| What is a Reversible inhibitors? | Substrate can bind and disassociate from enzyme. Structural similarity of substate and product |
| What is a competitive inhibitor? | Competes with substrate for binding on active site |
| Competitive inhibitor: What does a1, a2 and a3 identify? | a1 = no inhibitor (Km, substance concentration lowest) a2 = with inhibitor (Km higher) a3 = higher concentrated inhibitor |
| Uncompetitive inhibitor: What does a1, a1.5 and a2 identify? | a1 = no inhibitor a1.5 = with inhibitor (higher concentration of substrate and rate of reaction when saturated) a2 = higher concentrated inhibitor |
| Identify what type of enzyme inhibitor this graph is showing | Competitive inhibition |
| Identify what type of enzyme inhibitor this graph is showing | Uncompetitive inhibition |
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