Use LEFT and RIGHT arrow keys to navigate between flashcards;
Use UP and DOWN arrow keys to flip the card;
H to show hint;
A reads text to speech;
20 Cards in this Set
- Front
- Back
Carbohydrates |
-Consist of Carbon, Hydrogen and Oxygen
-Give quick Energy -Empirical Formula = (CH2O)n (n = # Carbons) -3 types: Monosaccharides, Disaccharides and Polysaccharides |
|
Monosaccharides (Carbohydrates) |
-Glucose, Galactose and Fructose |
|
Disaccharides (Carbohydrates) |
-Sucrose, Lactose and Maltose |
|
Polysaccharides (Carbohydrates) |
-Plants: Cellulose and Starch -Animals: Glycogen and Chitin |
|
Lipids |
-Consist of Carbon, Hydrogen and Oxygen -Comprise Fats, Oils, waxes and Steroids -Hydrophobic (not soluble in water) -Made of 1 Glycerol & 3 Fatty Acids (Except Steroids) -Functions: --> Energy Storage & Insulation --> Structure (Phospholipids make up Plasma Membrane) --> Endocrine: Some steroid are hormones |
|
Saturated Fatty Acid |
-Found in Animal Fat -All bonds between carbon atoms are single bonds |
|
Unsaturated Fatty Acid |
-Found in Plant Oil -Contains at least one double bond between carbons |
|
Steroid |
-Classified as a Lipid -Component of Plasma Membrane --> Makes Plasma Membrane less fluid, more stable -Non-Polar -Hydrophobic -Many are Sex Hormones in Vertebrates -Example: Cholesterol |
|
Proteins |
-Consist of: C, H, O, N, P, & S -Growth & Repair -Polymers consisting of Amino Acids -Each has a unique shape or conformation that determines its function -Chaperone Proteins help other proteins fold into the precise shapes -Denatured by High Temperatures and Acids |
|
Structures of Proteins |
-Primary Structure: Local - Peptide Bonds (Amino Acid Sequence) -Secondary Structure: Local - Hydrogen Bonding between 2 or more Primary Structures - Can be in Alpha, Beta Sheet or Beta Barrel shape -Tertiary Structure: Non-Local - 3-D shape, consists of peptide bonds, covalent disulfide bridges, ionic salt bridges, van der waals (hyrdophobic) and hydrogen bonding (hydrophilic) -Quaternary Structure: Consists of more than one Tertiary Structure, fold begins by hydrophobic collapse - covalent and charged interactions |
|
Nucleic Acids |
-RNA - Ribonucleic Acid -DNA - Deoxyribonucleic Acid -Polymers consisting of chains of nucleotides --> Nucleotides consists of: Sugar, Phosphate and a Nitrogenous Base |
|
Amino Acids |
-20 common or standard Amino Acids, classified into 4 categories --> Non-Polar (10) --> Polar (5) --> Basic (3) --> Acidic (2) -Each Amino Acids has 4 groups: COO-, an Amine, an H and an R Group |
|
Non-Polar Amino Acids |
"GAVLIMPPTT" -Glycine, Alanine, Valine, Leucine, Isoleucine, Methionine, Proline, Phenylalanine, Tyrosine, & Tryptophan --> Glycine and Alanine = "Bland AA's" --> Glycine = Most Common --> Methionine = Has a Sulfur --> Proline = Odd Duck (Forms a Ring) --> Aromatics = Phenylalanine, Tyrosine and Tryptophan --> Tyrosine = Has a Hydroxide |
|
Polar Amino Acids |
"GCATS" -Glutamine, Cysteine, Asparagine, Threonine & Serine --> Serine and Threonine = Have Hydroxide --> Asparagine and Glutamine = Have Amide --> Cysteine = Has a Thiol --> Cysteine = Most Reactive but Least Polar of the Polar Group |
|
Basic Amino Acids |
"LAH" -Lysine, Arginine & Histidine --> Lysine and arginine = Long primary Amine side chain --> Histidine = 5-membered Imidizol ring in side chain |
|
Acidic Amino Acids |
"GA" -Glutamate (Glutamic Acid), Aspartate (Aspartic Acid) --> Both = Additional COO- in side chain |
|
Characteristics of Enzymes |
-Organic catalysts -Control the rate of reactions -Lower activation energy, Increase Kinetics, Stabilize Transition State, but do not affect Thermodynamics -Assisted by Coenzymes (vitamins) and Cofactors (minerals) -Function based on Induced Fit Model -Denature above 40 C in humans |
|
Activation Energy |
-Energy required to begin a reaction |
|
Substrate |
-The molecule that an enzyme works on --> Ex: The enzyme Maltase catalyzes Maltose into Glucose ----> Maltose is the Substrate |
|
Standard Inhibition |
-Competitive Inhibition = Km changes, Vmax does not -Non-Competitive Inhibition = Vmax changes, Km does not -Uncompetitive Inhibition = Both the Km and Vmax Change --> All of the above display Michaelis Menten Kinetics |