AP Biology Biochemistry Vocabulary Flashcards

Terms Definitions
Alcohols
R-OH
carboxyl group
-COOH
hydrophilic
love water
intermolecular forces
...
triose
three carbon sugar
Anion
negatively charged ion
Starch
plants--storage of sugar/energy
enantiomer
synonym for optical isomer
ph of acid rain
1.5-5.4
monomers of nucleic acids
nucleotides
Ketone
contains an internal C=O group
unsaturated fat
fat with double bonds
Monosaccharide
Simplest kind of carbohydrate; consists of single sugar molecule such as glucose or fructose
Cofactors
Assist enzymes; include coenzymes (which are organic) and inorganic cofactors (usually metal ions)
covalent bonding
includes sharing of electrons
Function of Carbs:
primary energy nutrients
Polynucleotide
A polymer consisting of many nucleotide monomers in a chain; nucleotides can be those of DNA or RNA.
buffer
substance that resists changes in pH
disulfide bridge
tertiary structure; strong covalent bond formed when one sulfur of one cysteine monomer bonds to the sulfur of another
purine
adenine and guanine; six-membered ring fused to a five-membered ring
Chitin
Polymer of beta-glucose used for structure in fungi cell walls and in the exoskeletons of insects, arthropods, and mollusks
Cohesion
the binding together of like molecules, often by hydrogen bonds
monosaccharides
have a chemical formula of C6H12O6
examples are glucose, galactose, and fructose
Primary protein structure
sequence of amino acids
polar
a lack of symmetry; structural differences in opposite ends of an organism or structure
Structural Formula
an expanded molecular formula showing the arrangement of atoms within the molecule
bicarbonate ion
most important buffer in human blood
metabolism
sum of all chemical reactions that take place in cell
Enzymes
Proteins that act as catalysts for metabolic reactions; are substrate-specific; unchanged after the reaction; catalyzes a reaction forward and backwards; efficiency is affected by temperature and pH
Atomic Number
number of protons in an element
competitive inhibition
a phenomenon when some compounds resemble the normal substrate molecule and compete for the same active site on the enzyme. can be reversible or irreversible.
specificity
the arrangement of a protein (effects its actions)
composition of proteins
C, H, O, N, S
endergonic reaction
a nonspontaneous chemical reaction, in which free energy is absorbed from the surroundings
substrate
the reactant on which an enzyme works
Geometric Isomers
Compounds that have the same molecular formula but differ in the spatial arrangements of their atoms.
Specific Heat
the heat required to raise the temperature of one gram of a substance one degree centigrade
covalent bond
bond resulting from the sharing of electrons
ionic bond
bond resulting from a transfer of electrons
Induced-Fit Model
Substrate binds to active site of enzyme; enzyme changes shape to fit the substrate molecule better; reaction takes place; product is released
allosteric regulation
the binding of a regulatory molecule to a protein at one site that affects the function of the protein at different sites
competitive inhibitor
a substance that reduces the activity of an enzyme by entering the active site in place of the substrate whose structure it mimics
polar molecule
a molecule (such as water) with opposite charges on different ends of the molecule
Evaporative Cooling
the property of a liquid whereby the surface becomes cooler during evaporation, owing to a loss of highly kinetic molecules to the gaseous state.
surface tension
measure of how difficult it is to stretch or break the surface of a liquid
Allosteric Enzymes
Have a binding site for the substrate and a binding site for an allosteric effector
isotopes
atoms of one element that vary only in the number of neutrons in the nucleus. they are chemically identical.
hydrogen bonds
a type of weak chemical bond that's formed when the slightly positive hydrogen atom of a polar covalent bond in one molecule is attracted to the slightly negative atom of a polar covalent bond in another molecule
excited state
the state of an atom after that atom has absorbed energy and its electrons have moved to a higher energy level.
factors that contribute to a tertiary structure
1.hydrogen bonding between R groups of amino acids
2. ionic bonding between R groups
3.hydrophobic interactions
4.van der waals interactions
5.disulphide bonds between cysteine amino acids
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