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Description
Flashcards by Charlotte Willis, updated more than 1 year ago
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Created by Charlotte Willis
over 6 years ago
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| Question | Answer |
| Two types of Proteins | Globular and Fibrous |
| What are Globular proteins? | Soluble proteins with specific 3D shape e.g Hormones, Enzymes, Haemoglobin, Antibodies |
| What are Fibrous proteins? | Strong, insoluble, flexible material E.g Collagen and Keratin |
| Building Blocks for Proteins? | Amino Acids |
| Structure of Amino Acid? | -Central Carbon -Carboxyl (COOH) Group to right -Amino Group to Left -Hydrogen above -R Group below |
| How do amino acids differ? | The R group varies |
| How do amino acids join together? | Condensation reaction between Carboxyl group and amino group. Peptide Bond |
| What does two amino acids form? | Dipeptide |
| Monomers of Proteins | Amino Acids |
| What are Proteins made up of? | One or more Polypeptides |
| Define the Primary Structure | Sequence of amino acids - Polypeptide chain |
| Define the Secondary structure | Hydrogen bonds between the amino acids form coils - alpha helix OR Beta pleated sheets |
| Define the Tertiary structure | The coiled structures coil more due to hydrogen and ionic bonds between amino acids. Disulphide bridges between Cystine amino acids If the structure only have ONE polypeptide bond this is the final 3D structure |
| Define the Quaternary Structure | Several different polypeptide chains bonded together Final 3D structure for proteins made of more than one polypeptide chain ( Haemoglobin, Insulin, Collagen |
| Test for Protein | Biuret test Add Sodiumhydroxide solution Add Copper (II) Sulfate solution Protein turns from blue to purple |
| Define an Enzyme | AN biological Catalyst Speed up the rate of reaction - lower activation energy |
| What makes a Enzyme specific? | Specific active shape Only complementary substrates can bind to it |
| Structure of Enzymes | -Rough spherical shape due to tight folding of polypeptide chains. -Soluble -Roles in Metabolism or Synthesis of large molecules |
| Structure and role of Antibodies | -Involved in Immune response -Two light (short) polypeptide chains and two heavy (long) polypeptide chains -Have variable regions |
| Structural Proteins | -Physically Strong -Consist of long polypeptide chains that lie parallel to each other w/ crosslinks between them - Include Keratin (In hair and nails) and Collagen (connective tissue) |
| Lock and Key Model Vs Induced Fit Model | L+k - Active site shape is rigid, only exact complementary substrates can bind to form Enzyme-Substrate complexes I F - Active site changes shape, substrate binds to act site, active site changes shape so the substrate fit exactly forming Enzyme-substrate complex |
| Affect of Substrate concentration on enzyme activity | - Increase substrate concentration = -Increase chance of successful collisions -Increase chance of forming an enzyme substrate complex -Increase rate of reaction -Continues until all enzymes are satisfied |
| Affect of enzyme concentration on enzyme activity | Increase enzyme concentration = -increase chance of successful collisions -increase chance of forming an Enzyme- substrate complex -increase R of R -this continues until all substrates are used up + max. R of R |
| Affect of temp on enzyme | Temp increases = -increase R of R -Kinetic energy increases -Molecules move faster -Increase chance of successful collisions and Enzyme-substrate complex -caries until optimum After Optimum = -Decrease R of R -Bonds in tertiary structure break -Lose Active site -enzyme denatured |
| Affect of pH on enzyme activity | Change in pH away from optimum = -Bonds in tertiary structure break -Lose active site -Denatured enzyme - No Enzyme-Substrate complex |
| Competitive VS non-competitive inhibitors | - C = - A substance with a similar shape to substrate w/ complementary shape to enzyme active shape -Binds to active site, block it, prevent ES complexes forming N-C = - Substance that binds to another site on the enzyme other then the active site, changing the active site shape - |
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