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84 Cards in this Set

  • Front
  • Back
consist of positively charges protons and neutrally charged neutrons with negatively charged electrons arranged outside the nucleus
groups of two or more atoms held together by chemical bonds
Chemical Bonds
interaction of electrons
ability of an atom to attract electrons
Ionic Bond
when one or more electrons are transferred from one atom to the other or when there is a large difference in electronegativities.
Covalent Bond
forms when electrons are shared
Non-polar Covalent Bond
forms when electrons are shared equally
forms when electrons are shared unequally
When electrons form a bond around the atom with greater electronegativity, a negative charge is produced. Also known as a pole.
Hydrogen Bonds
Weak bonds that form between two molecules when a positively charged hydrogen atom is attracted to a negatively charged area of another atom.
Why is water a good solvent?
Polar water molecules can interact with ionic substances and separate them into ions.
"Water Loving."
"Water Fearing." Substances that lack charged poles do not dissolve in water and are thus hydrophobic.
Define Heat Capacity and describe why it is beneficial for water to have a high heat capacity.
Heat Capacity is the degree to which a substance changes temperature in response to a gain or loss of heat. Water has a high heat capacity, which means that its temperature changes very slowly and that it takes a lot of energy to heat or cool water.
Why does ice float?
water expands as it freezes, thus it is more dense in the solid form.
Define Cohesion and describe why water has strong cohesion.
Cohesion is the attraction between like substances and the hydrogen bonds in water are what give water its strong cohesion, eventually giving it high surface tension.
attraction of unlike substances
Capillary Action
Water displays capillary action by rising up tubing or creeping through paper.
hydroxyl group - polar and hydrophilic
Carboxyl group - polar and hydrophilic
amino group - polar and hydrophilic
PO3 2-
Phosphate group - polar and hydrophilic
CO (end)
Carbonyl (Ketone)
CO (Middle)
Carbonyl (Aldehyde)
Methyl - nonpolar and hydrophobic
Name the three divisions of carbohydrates
Monosaccharides, Disacharides, and Polysaccharides
single sugar molecule with the formula (CH20)n
two sugar molecules
Glycosidic Linkage
bond between two sugars that results in the loss of water (aka dehydration reaction)
a series of monosacharrides
polymer of alpha glucose. Serves as energy storage in plants
polymer of alpha glucose. Serves as energy storage in animals. Branching is different that starch.
polymer of beta glucose. Serves as a structural molecule in plant cell walls.
polymer of beta glucose, but has a nitrogen group attached to the ring. Serves as a structural molecule in the walls of fungus or exoskeletons of insects.
Describe some properties of lipids and name the three main groups of lipids
Lipids are insoluble in water. Three main groups are triglycerides, phospholipids, and steroids
consist of three fatty acids attached to a glycerol molecule
Saturated Fatty Acid
has a single covalent bond between each pair of carbon atoms.
Monounsaturated Fatty Acid
has one double covalent bond
Polyunsaturated Fatty Acid
has two or more double covalent bonds
looks like a lipid except one of the fatty acid chains is replaced with a phosphate group, thus there is a phosphate "head" and fatty acid "tails"
has both polar and nonpolar regions
contain a backbone of four linked carbon rings
Name 5 Major protein categories
Structural, Storage, Transport, Defensive, and Enzymes
What are proteins?
Proteins, also known as polypeptides, are polymers of amino acids held together by peptide bonds
What is the structure of an amino acid?
A central carbon bonded to an amino group, a carboxyl group, a hydrogen, and a functional R group
Primary Structure of Proteins
order of amino acids
Secondary Structure of Proteins
3D shape formed from hydrogen bonds between amino and carboxyl groups of adjacent amino acids. Most secondary structures result in the alpha helix or beta pleated sheet.
Fibrous Proteins
Proteins dominated by either the alpha helix or beta pleated sheet structures.
Tertiary Structure of Proteins
additional 3D shaping aqnd often dominates the structure of globular proteins
What factors contribute to tertiary structure?
Hydrogen Bonding, Ionic Bonding, Hydrophobic Effect (when hydrophobic R groups move toward the center), and formation of disulfide bonds.
Quaternary Structure
protein that is assembled from two or more polypeptide chains
What is DNA?
Also known as Deoxyribonucleic Acid, DNA is a polymer of nucleotides
What do nucleotides consist of?
Nitrogen base, five carbon sugar (deoxyribose), and a phosphate group
Name the 4 DNA nucleotides?
Adenine, Thymine, Cytosine, Guanine
single ring sugar base
double ring sugar base
What is the grouping of the nucleotides? That is, which can bond to which?
Adenine and Thymine, Cytosine and Guanine
What does it mean for DNA to be antiparallel?
Antiparallel means that each strand is oriented in opposite directions, one is from the 5'-->3' direction while the other is 3'-->5'
How does RNA differ from DNA?
the sugar is ribose, thymine does not exist in RNA, it is replaced with uracil, and it is single stranded
Activation Energy
Energy required to trigger thr formation of new bonds
lowers the activation energy required for a reaction to take place
chemical reactions that occur in biological systems
the breakdown of substances
formation of new products
formation of new products
when the rate of the forward reaction equals the rate of the reverse reaction
globular proteins that act as catalysts for metabolic reactions
substance(s) upon which the enzyme acts
Induced Fit Model (Lock and Key)
within the enzyme, there is an active site with which reactants readily interact because of the shape, polarity, or other characteristics of the active site.
What two factors cause enzymes to lose their functionality?
Temperature and pH
What is the standard suffix for enzymes?
nonprotein molecules that assist enzymes
union of cofactor and enzyme (apoenzyme when joined together)
organic cofactors that usually function to donate or accept some component of the reaction, often electrons
Inorganic Cofactors
often metal ions
Adenosine Triphosphate is a common source of activation energy for metabolic reactions
when new ATP molecules are assembled via ADP+phosphate
What is an allosteric enzyme and describe its function
they help regulate chemical reactions. They have two binding sites, an active site for substrates and an allosteric site for an allosteric effector
Allosteric Activator
binds to the enzyme and induces the enzymes active form
Allosteric Inhibitor
binds to the enzyme and induces the enzyme's inactive form
Feedback Inhibition
an end product of a series of reactions that acts like an allosteric inhibitor
Competitve Inhibition
substance that mimics the substrate and occupies the active site
Noncompetitive Inhibitor
binds to an enzyme at locations other than an active or allosteric site and causes the enzyme to change shape and lose functionality
an enzyme becomes more receptive to additional substrate molecules after one substrate molecule attaches to an active site.