• Shuffle
    Toggle On
    Toggle Off
  • Alphabetize
    Toggle On
    Toggle Off
  • Front First
    Toggle On
    Toggle Off
  • Both Sides
    Toggle On
    Toggle Off
  • Read
    Toggle On
    Toggle Off
Reading...
Front

Card Range To Study

through

image

Play button

image

Play button

image

Progress

1/20

Click to flip

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