One unit of positive charge. Approximately one dalton. Located in nucleus.
Back
Molecule
Front
Two or more atoms held together by covalent bonds.
Back
Products
Front
The resulting material of a chemical reaction.
Back
Ionic Compounds
Front
Or Salts. Compounds formed by ionic bonds.
Back
Double Bond
Front
Sharing two pairs of valence electrons.
Back
Isotopes
Front
Same number of protons, but different number of neutrons and therefore different mass. Same element.
Back
organic chemistry
Front
The study of carbon & hydrogen compounds (organic compounds).
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Electron Shells
Front
Where electrons are found, each with characteristic average distance and energy level. Electrons can change these by absorbing or losing energy.
Back
Atomic Nucleus
Front
Dense core packed with protons and neutrons.
Back
Chemical Equilibrium
Front
The point at which the relative concentrations of the products and the reactants stop changing and offset one another exactly.
Back
Ionic Bonds
Front
The attraction of cations and anions. The transfer of electrons creates ions which form an ionic bond.
Back
isomer
Front
One of several compounds with the same molecular formula but different structures and therefore different properties. The three types are structural, geometric, and enantiomers.
Back
Polar Covalent Bond
Front
Where one atom is bonded to a more electronegative atom and the electrons of the bond are not shared equally.
Back
testosterone
Front
Asteroid hormone required for development of the male reproductive system, spermatogenesis, and male secondary sex characteristics; the major androgen in mammals.
Back
Valence
Front
Bonding capacity. Equal to the number of unpaired electrons required to complete the outermost (valence) shell.
Back
functional groups
Front
A specific configuration of atoms commonly attached to the carbon skeletons of organic molecules and involved in chemical reactions.
Back
Element
Front
Substance that cannot be broken down to other substances through chemical reactions. Each has a symbol. 92 occurring in nature.
Back
Covalent Bond
Front
Sharing of a pair of valence electrons by two atoms.
Back
Potential Energy
Front
Energy matter possesses because of its location or structure. Electrons have this based on distance from nucleus.
Back
Neutrons
Front
Electrically neutral. Approximately one dalton.
Back
Chemical Bonds
Front
The attraction that holds atoms together during an interaction.
Back
Electronegativity
Front
The attraction of a particular kind of atom for the electrons of a covalent bond.
Back
enantiomer
Front
One or two compounds that are mirror images of each other and that differ in shape due to the presence of an asymmetric carbon. (MIRROR IMAGE)
Back
Structural Formula
Front
H--H. Notation which represents both atoms and bonding.
Back
Nonpolar Covalent Bond
Front
Covalent bond in which electrons are shared equally.
Back
geometric isomer
Front
One of several compounds that have the same molecular formula and covalent bonds between atoms but differ in the spatial arrangements of their atoms owing to the inflexibility of double bonds (DIFFERENT ARRANGEMENT)
Back
Matter
Front
Anything that takes up space and has mass.
Back
Cation
Front
A positively charged atom.
Back
Atomic Number
Front
The number of protons (which is unique to that element) and written as a subscript to left of element symbol. Also tells us number of electrons since P=E if atom is neutral
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Trace Elements
Front
Required by an organism only in minute quantities.
Back
Hydrogen Bond
Front
When a hydrogen atom covalently bonded to an electronegative atom is also attracted to another electronegative atom.
Back
hydrocarbon
Front
An organic molecule consisting only of carbon and hydrogen.
Back
Atom
Front
Smallest unit of matter that retains the properties of an element. Composed of subatomic particles. Mostly empty space.
Back
Compound
Front
Substance consisting of two or more different elements combined in a fixed ratio.
*Characteristics different than those of its elements
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Mass Number
Front
Sum of the protons and the neutrons. An approximation of the atomic mass.
Back
Ion
Front
A charged atom.
Back
estradiol
Front
A steroid hormone that stimulates the development and maintenance of the female reproductive system and secondary sex characteristics; the major estrogen in mammals.
Back
Energy
Front
Capacity to cause change
Back
Subatomic particles
Front
Neutrons, protons, electrons. Make up atoms.
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Molecular Shape
Front
Determines how biological molecules recognize and respond to one another.
Back
Electron
Front
One unit of negative charge. Located outside of nucleus.
Back
Radioactive Isotope
Front
One in which the nucleus decays spontaneously, giving off particles and energy. Can decay to a different element. Have useful applications.
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Reactants
Front
The starting materials of a chemical reaction.
Back
CHON
Front
4 elements essential to life
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carbon
Front
this atom has 4 electrons in valence shell and can form 4 covalent bonds with other atoms
Back
Anion
Front
A negatively charged atom.
Back
structural isomer
Front
One or several compounds that have the same molecular formula but differ in the covalent arrangement of their atoms. (DIFFERENT SHAPE)
Back
Valence Electrons
Front
Electrons in the outermost shell.
Back
van der Waals Interactions
Front
Ever changing regions of positive and negative charge that enable all atoms and molecules to stick to one another.
Back
Single Bond
Front
One pair of shared electrons.
Back
Section 2
(50 cards)
Cellulose
Front
Polymer of β glucose monomers that is found in plant cell walls
Back
Sickle cell anemia
Front
In this disease, one amino acid at the primary level (valine) replaces glutamic acid and the result is a distorted shape at the subsequent levels.
Back
Metabolism
Front
All the chemical conversions that occur within a cell
Metabolism = anabolism + catabolism
Back
aldehyde group
Front
A chemical group consisting of a carbon double bonded to oxygen and single bonded to hydrogen (must be at end of chain)
Back
HDL
Front
Good cholesterol is called ___ ____________.
HINT: Keep your ____ HIGH :-)
Back
3D structure
Front
The amino acid sequence ultimately determine the __ _________ of proteins.
Back
Monosaccharide
Front
The monomer in a carbohydrate is a(n) ______________.
EX: Glucose
Back
ketone group
Front
A chemical group consisting of a carbon double bonded to oxygen (must be in middle of chain)
Back
Unsaturated fats
Front
Fats with one or more double covalent bonds, which is less likely to solidify and more flexible.
Back
amino group
Front
A chemical group consisting of a nitrogen atom bonded to two hydrogen atoms can act as a base in solution, accepting a hydrogen ion and acquiring a charge of 1⁺
Back
sulfhydryl group
Front
A chemical group consisting of a sulfur atom bonded to a hydrogen atom.
Back
α glucose
Front
Starch and glycogen are polymers of ________ molecules.
Back
Polymers
Front
Lipids are the only large biological molecules that do not form __________.
Back
Glycogen; starch
Front
Stored carbohydrate in an animal is called ________; in a plant, it is ______.
Back
Tertiary
Front
At the ________ level of protein structure, various chemical associations in precise regions of a polypeptide cause it to fold into a 3D shape that will determine its function.
Back
Hydrolysis
Front
Pocess that is the reverse of dehydration synthesis. In __________, or water breakage, the bond between monomers is broken by the addition of a water molecule.
Back
LDL
Front
The bad cholesterol, which can harden in arteries.
HINT: Keep your ____ LOW :-)
Back
Disaccharide
Front
Two monosaccharides covalently bonded form a ____________.
EX: Sucrose
Back
Polysaccharide
Front
Three or more monosaccharides linked together form a ______________.
Back
phosphate group
Front
A chemical group consisting of a phosphate atom bonded to four oxygen atoms; important in energy transfer.
Back
Primary
Front
At the _______ level of protein structure, a linear sequence of amino acids is joined by peptide bonds to form a polypeptide.
Back
Carbohydrates, proteins, lipids, and nucleic acids
Front
Name the 4 types of macromolecules
Back
hydroxyl group
Front
A chemical group consisting of an oxygen atom joined to a hydrogen atom. Molecules possessing this group are soluble in water and are called alcohols.
Back
Glycosidic linkage
Front
The bond in a carbohydrate is a(n) __________ _______.
Back
Polymers
Front
Long molecules consisting of many similar or identical building blocks linked by covalent bonds.
Back
Chitin; cellulose
Front
Two examples of structural carbohydrates are ______ and _________.
Back
Dehydration synthesis
Front
Reaction in which two molecules are covalently bonded, with the loss of a water molecule
Back
Phospholipid
Front
Basic structural component of cell membranes, with a polar/hydrophilic head region and a nonpolar/hydrophobic tail region, giving membranes their selective permeability.
Back
Secondary
Front
At the _________ level of protein structure, hydrogen bonds form between the partial positive hydrogen atom of amine groups and the partial negative oxygen atom of carboxyl groups.
Back
Catabolism
Front
Conversion of complex organic molecules into smaller molecules by breaking chemical bonds
Back
Lipids
Front
Cushioning of organs, insulation, and energy storage are three functions of ___________.
Back
ester group
Front
A chemical group consisting of a carbon double bonded to oxygen and single bonded to another oxygen (must be in middler of chain)
Back
Amino; carboxyl; R
Front
Amino acids are formed of a(n) _____ group with a(n) ________ group and a(n) _ group side chain.
Back
Peptide
Front
In a _______ bond, the ---COOH group in one amino acid loses an ---OH and the ---NH2 group in another amino acid loses a H.
Back
Glycosidic linkage
Front
In carbohydrates, monosaccharides are joined together in a covalent bond called __________ _______.
Back
α Helix
Front
___ ___________ are a secondary structure found in proteins.
Back
Structure
Front
A protein's _________ determines its function.
Back
Steroid
Front
Lipid characterized by a carbon skeleton consisting of hydrogen-fused rings.
Back
Monosaccharides
Front
Carbohydrates are made up of _______________.
Back
20
Front
# different amino acids which can assemble according to genetic code to make different proteins.
Back
Anabolism
Front
Conversion of small organic molecules by forming chemical bonds between smaller molecules
Back
Hormonal
Front
Insulin and glucagon are examples of _________ proteins.
Back
Quaternary
Front
At the __________ level of protein structure, 2 to 4 completely formed polypeptides combine.
Back
Amino acid
Front
The monomer in a protein is a(n) _____ ____.
Back
ionized carboxyl group
Front
A chemical group consisting of a single carbon atom double-bonded to an oxygen atom and also bonded to a negatively charged oxygen
Back
Glycerol; fatty acid chains
Front
Triglyceride is composed of a ______ and three ____ _____ ______.
Back
β Pleated Sheet
Front
__ ___________ ______________ are a secondary structure found in proteins.
Back
Ester linkage
Front
In a triglyceride, the ---OH of glycerol loses a H and the ---COOH of the fatty acid chain loses a ---OH which joins to form water in a(n) _____ _______.
Back
Polypeptide
Front
The polymer in a protein is a(n) ___________.
Back
carboxyl group
Front
A chemical group consisting of a single carbon atom double-bonded to an oxygen atom and also bonded to a hydroxyl group
Back
Section 3
(47 cards)
Transport
Front
_____________ proteins move molecules into and out of cells.
Back
Calorie
Front
amount of heat it takes to move 1 gram of substance 1 degree Celsius higher
Back
hydronium ion
Front
H30+
Back
Cohesion
Front
holding a substance together
Back
Receptor
Front
________ proteins are embedded in all membranes and allow cells to interact with molecules and other cells.
Back
Phosphodiester bonds
Front
Nucleotides link together via ________ _____ to form nucleic acid.
Back
buffers
Front
substance that minimizes changes in H+/OH- concentration
Back
solution
Front
liquid completely homogeneous of two or more substances
Back
molarity
Front
concentration measured by number of mols/liter of solution
Back
Nucleotides
Front
Nucleic acids are composed of ___________.
Back
acids
Front
increase H+ concentration
Back
hydroxide ion
Front
OH-
Back
Adhesion
Front
clinging of a substance to another
Back
mole
Front
the molecular weightof a substance expressed in grams (6.02 x 10^23)
Back
A, T, C, G
Front
The nitrogenous bases in DNA are ____.
Back
vaporization
Front
amount of heat needed to turn liquid into gas
Back
deoxyribose
Front
The sugar in DNA is ______.
Back
solvent
Front
dissolving agent
Back
Ribose
Front
The sugar in RNA is ______.
Back
evaporation
Front
process of liquid becoming gas
Back
acid precipitation
Front
presence of sulfur oxides/nitrogen oxides and gaseous compounds react with air and goes into lakes, oceans, and soil, affecting animal life
Back
bases
Front
reduce H+ concentration
Back
polar covalent
Front
type of bond in water? Oxygen is more electronegative than hydrogen and the electrons of the polar bonds spend more time near oxygen thus, making oxygen more negativity charged and hydrogen more positively charged
Back
hydrophilic
Front
water loving substances
Back
How does the density of water contribute to aquatic life?
Front
if ice sank, ponds/oceans/lakes would freeze solid, killing the life (during the summer only top would thaw) instead the floating ice insulates liquid water from below preventing it from freezing and killing animals
Back
Heat
Front
total kinetic energy due to molecular motion
Back
hydrophobic
Front
water hating substances
Back
A, U, C, G
Front
The nitrogenous bases in RNA are ____.
Back
Kinetic Energy
Front
energy of motion
Back
Evaporative cooling
Front
remains of a liquid cool down
Back
Chaperonins
Front
Assist in the proper folding of the protein by keeping the polypeptide segregated from disruptive chemical conditions in the cytoplasmic and create a hydrophilic environment for folding polypeptides
Back
Polynucleotide
Front
The polymer in a nucleic acid is a(n) ______________.
Back
aqueous solution
Front
water is solvent
Back
Capillary action
Front
the attraction of the surface of a liquid to the surface of a solid, which causes the liquid to rise or fall
Capillary action is the ability of a liquid to flow in narrow spaces without assistance.
It occurs because of intermolecular forces between the liquid and surrounding solid surfaces.
If the diameter of the tube is sufficiently small, then the combination of surface tension (which is caused by cohesion within the liquid) and adhesive forces between the liquid and container wall act to propel the liquid.
When adhesion > cohesion, capillary action occurs.
Back
solute
Front
substance dissolved
Back
Specific heat
Front
amount of heat needed to be absorbed /lost to change the temperature by 1 degree Celsius
water has a high _____.
Back
hydration shell
Front
sphere of water molecules around dissolved ions
Back
Defensive
Front
_________ proteins, like antibodies, are produced in response to antigens and bind to them.
Back
water
Front
1 calorie/1 gram/I degree Celsius is the specific heat of ____.
Back
hydrogen ion
Front
H+
Back
pH scale
Front
measures concentration of H+ (scale from 1-14)
Back
sugars; phosphate groups
Front
The backbone of DNA and RNA molecules is composed of alternating _____________ and ______________.
Back
Hydrogen
Front
Nitrogenous bases in DNA and RNA form complementary base pairs by forming ____________ bonds.
Back
Contractile/Movement
Front
___________ proteins, such as actin and myosin, are found in muscle cells.
Back
Temperature
Front
intensity of heat due to average kinetic energy
Back
Denaturation
Front
Excessive heat can cause ____________, in which a protein unravels and loses its native shape.
Back
Surface Tension
Front
A measure of how difficult it is to break/stretch a surface