• 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

1/32

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;

32 Cards in this Set

  • Front
  • Back
Monomers of nucleic acids
Nucleotides (be able to draw one)
Monomers of proteins
Amino acids (be able to draw one)
Structure of carbohydrates
1:2:1 ratio between carbon, hydrogen, and oxygen
Most common elements in living things
carbon (C), hydrogen (H), oxygen (O), nitrogen (N)
Elements important to living things
sulfur (S), calcium (Ca), phosphorus (P), iron (Fe), sodium (Na)
Properties of water
Polar, cohesive, has high specific heat, and is an excellent solvent.
Organic Molecules
Contain carbon and hydrogen and are found in living organisms.
monosaccharides
glucose, galactose, fructose
disaccharides
maltose, lactose, and sucrose
disaccharides
maltose, lactose, and sucrose
polysaccharides
starch, glycogen, and cellulose
Draw me!
amino acid
Draw me!
glucose
Draw me!
fatty acid
Draw me!
nucleotide
condensation reaction
two monomers react to form a dimer, water is a product.
hydrolysis reaction
one dimer (or polymer) becomes two monomers, water is a product.
functions of lipids
energy storage, thermal insulation, protection of internal organs, major component of cell membranes.
function of amino acids
create proteins
functions of carbohydrates
energy and structural support
functions of nucleotides
passage of genetic information from parent to offspring, creation of proteins.
function of proteins
structural support, transport, movement, defence, metabolism
globular proteins
water soluble, have round (globby) shape.
Enzymes are typically globular proteins
fibrous proteins
water insoluble, long, stringy shape.
Collagen is an example of a fibrous protein
enzymes
proteins that catalyze chemical reactions.
allosteric inhibition
enzyme inhibition caused by binding to a site other than the active site
competitive inhibition
enzyme inhibition caused by binding of an inhibitor to the active site, blocking the substrate
coenzyme
a molecule (often a vitamin) that increases enzyme activity by binding to an allosteric site.
Primary Protein Structure
Order of amino acids. Peptide bonds hold amino acids together.
Secondary Protein Structure
Repeated "motifs" or patterns in the polypeptide that form either a helix or a pleated sheet. Stabilized by hydrogen bonds.
Tertiary Protein Structure
Interactions between the variable "R" groups that cause the polypeptide's "nascent" folded form. Bonds can be ionic, covalent, hydrogen, or disulfide.
Quaternary Protein Structure
Interactions between several polypeptides to form the completed and functioning protein.