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122 Cards in this Set

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These consist of a nucleus of positively charged protons and neutrally charged neutrons (outside of the nucleus).
Groups of two or more atoms held together by chemical bonds.
Chemical Bonds
Bonds that form between atoms because of interaction of their electrons.
______ of an atom, or the ability of an atom to attract electrongs, plays a large part in determining the kind of bond that forms.
These bonds form between two atoms when one or more electrons are TRANSFERRED from one atom to another. It occurs when the electronegativities of tha atoms are very different and one atom has a stronger pull (high electronegativity).
Atoms with a positive or negative charge. The atom that gains electrons has an overall negative charge, and the atom that loses electrons has an overall positive charge. Negatives and positives attract.
These bonds form when electrons between atoms are SHARED, which means that neither atom completely retains possession of the atoms
(as happens with atmos that form strong ionic bonds). These occur when the electronegativities are similar.
These bonds form when electrons between atoms are SHARED, which means that neither atom completely retains possession of the atoms
(as happens with atmos that form strong ionic bonds). These occur when the electronegativities are similar.
Nonpolar Covalent
Bonds that form when electrons are SHARED EQUALLY. When the two atoms sharing electrons are identical, such as in oxygen gas, the electronegativities are identical and both atoms pull equally on the electrons.
Polar Covalent
Bonds that form when electrons are SHARED UNEQUALLY. Atoms in this kind of bond have electronegativities that are different and an unequal distribution of the electrons result.
Negative charge near the atom produced by the electrons forming the polar covalent bond closer to the atom with the greater electronegativity. The atom with the low elect. has a positive pole.
Single, Double, Triple Covalent
Bonds that form when two, four, and six electrongs are shared, respectively.
Bonds that are weak bonds between MOLECULES. They form when a positively charged hydrogen atom in one covalently bonded molecule is attracted to a negatively charged area of another covalently bonded molecule.
Water is an excellent one. Ionic substances are _____ (they dissolve) in water because the poles of the polar water molecules interact with the ionic substances and separates them into ions. Polar covalent bonds are also soluble because of the interaction of their poles with those of water.
Substances that dissolve in water (Ionic and Polar Covalent bonds)
Substanes that do not dissolve in water because they lack charged poles (nonpolar covalent bonds).
Heat Capacity.
Water has a high ______. It is the degree to which a substance changes temperature in response to a gain or loss in heat. If it is high then the temperature changes very slowly with changes in its heat content.
Frozen Water
Ice floats. Unlike most substances that contract and become more dense when they freeze, water EXPANDS as it freezes and becomes less dense than in liquid form. The wek hydrogen bonds between water molecules becomes rigid and form a crystal that keeps the molecules separated and less dense.
Cohesion/ Surface Tension
Water has strong ____1___ and high ___2____. The attraction between LIKE substances is ____1_____ and it occurs in water because of the hydrogen bonding. Strong ____1___ between water molecules produces a high __2___.
Water adheres to other molecules. This is the attraction of UNLIKE substances.
Capillary Action
When water adheres to the walls of narrow tubing or to absorbent solids like paper, it demonstrates this by rising up tubing or creeping through paper.
These types of molecules have carbon atoms.
In living systems, large organic molecules that may consist of hundreds or thousands of atoms.
What most macromolecules are, which are molecules that consist of a single unit (monomer) repeated many times.
A single unit of a polymer.
Carbon forms....
It forms four covalent bonds with other atoms.
Functional Groups
Organic molecules that share similar properties because they have similar clusters of atmos. It gives a property such as acidity or polarity.
Alcohols like ethanol, glycerol, sugars that are polar and hydrophilic.
Carboxylic acids like acetic acid, amino acids, fatty acids, sugars that are polar, hydrophilic, and are weak acids.
Amines that include amino acids that are polar, hydrophilic, and are a weak base.
Orgnic phosphates that include DNA, ATP, and phospholipids that are polar, hydrophilic, and an acid.
Ketones that include acetone, sugars and are polar and hydrophilic.
Aldehydes that include formaldehydes and sugars and are polar and hydrophilic.
Includes fatty acids, oils, and waxes and are nonpolar and hydrophobic.
These are classified into three groups according to the number of sugar (or saccharide) molecules present. The groups are monosaccharaides, disaccharides, and polysaccharides.
The simplest kind of carbohydrate. It consists of a single sugar molecule, such as fructose or glucose. Sugar molecules have the formula (CH2On) where n is any number from 3 to 8. And a carbon molecule is present wherever four lines are joined.
-Glucose and -Glucose
These two forms of glucose differ simply by a reversal of the H and OH on the first carbon.
Consists of two sugar molecules joined by glycosidic linkage. Common ones are glucose+fructose=sucrose (common table sugar), glucose+galactose=lactose (sugar in milk), glucose+glucose=maltose.
Glycosidic Linkage
Link between two sugar molecules when a disaccharide is formed. During the process of joining, a water molecule is lost.
Type of chemical reaction where a simple molecule is lost, like in glycosidic linkage.
Condenstation reaction when the lost molecule is water.
glucose+fructose, common table sugar
Glucose+Galactose, the sugar in milk
A series of connected monosaccharides. It's a polymer because it consists of repeating units of a monosaccharide.
Polymer of Alpha-Glucose molecules. It is the principle ENERGY STORAGE molecule in plant cells.
Polymer of Alpha-Glucose. It differs from starch by its pattern of polymer branching. It is a major ENERGY STORAGE molecule in animal cells.
Polymer of Beta-Glucose molecules. It serves as a STRUCTURAL molecule in the walls of plant cells and is the major component of wood.
A polymer similar to cellulose, but each Beta-Glucose molecule has a nitrogen-containing group attatched to the ring. It serves as a STRUCTURAL molecule in the walls of fungus cells and in the exoskeletons of insects, other arthropods, and mollusks.
A class of substances that are insolubable in water (and other polar solvents) but are soluble in nonpolar substances (like ether or chloroform). There are three major groups of lipids which include triglycerides, phospholipids, and steroids.
These include fats, oils, and waxes. They consist of three fatty acids attached to a glycerol molecule.
Fatty Acids
Hydrocarbonds (chains of covalently bonded carbons and hydrogens) with a carboxyl group (-COOH) at one end of the chain. They vary in structure by the number of carbons and by the placement of single and double covalent bonds between the carbons.
Type of fatty acid that has ONE DOUBLE covalent bond and each of the two carbons in this bond has only one hydrogen atom bonded to it.
Type of fatty acid that is like a monounsaturated fatty acid except that there are TWO OR MORE DOUBLE covalent bonds.
It looks just like a lipid except that one of the fatty acid chains is replaced by a phosphate group ( ). An additional chemical group (R) is usually attached to the phosphate group. The two fatty acid "tails" are nonpolar/hydrophobic and the phosphate "head" is polar and hydrophilic. They make up cell membranes.
Another term for a phospholipid because it has both polar and nonpolar regions. They are often found oriented in sandwichlike formations with the hydrophobic tails grouped on the inside and the hydrophilic heads on the outside facing an aqueous envirment.
Phospholipid Structural Formula and Symbol
Characterized by a backbone of four linked carbon RINGS. Examples include cholesterol (a component of call membranes) and certin hormones, including testosterone and estrogen.
Steroid Pictures
Sugar Pictures
Lipid Pictures
Proteins can be grouped according to their function. Major categories include structural proteins, storage proteins, transport proteins, defensive proteins, and enzymes.
Structural Proteins
Includes keratin in the hair and horns of some animals, collagen in connective tissues, and silk in spider webs.
Storage Proteins
Includes casein in milk, ovalbumine in eggwhites, and zein in corn seeds.
Transport Proteins
Includes proteins in the membranes of cells that transport materials in and out of cells and as oxygen-carrying hemoglobin in red blood cells.
Defensive Proteins
Includes the antibodies that provide protection against foreign substances that enter the bodies of animals.
Proteins that regulate the rate of chemical reactions.
Amino Acids
Creates a covalently bonded chain so that proteins are polymers of this.
Peptide Bonds
Bonds between amino acids
Chain of Amino Acids connected with Peptide Bonds
Another name for Polypeptide
Components of an Amino Acid
A central carbon bonded to an amino group (-NH2), a carboxyl group (-COOH), and a hydrogen atom. The fourth bond is R which stands for Radical (a group of atoms or an atmo that varies from one amino acid to the next).
Amino Acid (General Formula)
Primary Structure
Describes the order of amino acids in a protein. (Cys-Tyr-Phe-Asn....)
Secondary Structure
The 3-D shape of a protein that results from hydrogen bonding between the amino and carboxyl groups of adjacent amino acids.
Alpha Helix
When the secondary structure forms a spiral.
Beta Pleated Sheet
When the secondary structure forms a folded plane like the pleats of a skirt.
Fibrous Proteins
Proteins whose shape is dominated by Alpha helixes ad Beta pleated sheets.
Tertiary Structure
The additional 3-D shaping of a protein and it often domindates the structure of globular proteins.
Components of Tertiary Structure
1. Hydrogen bonding between R groups of amino acids
2. Ionic bonding between R groups of amino acids
3. The hydrophobic effect that occurs when hydrophobic R groups move toward the center of the protein and away from the water in which the protein is usually immersed
4. Formation of Disulfide bonds
Disulfate Bonds
Helps create tertiary structure when the sulfer atom in the amino acid cysteine bonds to the sulfer atom in another cysteine (forming cystine, a kind of "double" amino acid). This helps maintain turns of the amino acid chain.
Quaternary Structure
Describes a protein that is assembled from two or more seperate peptide chains. The globular protein hemoglobin, for example, consists of four peptide chains that are held together by hydrogen bonding, interactions among R groups, and disulfide bonds.
Nucleic Acids
The genetic information of a cell is stored in molecules of deoxyribonucleic acid (DNA). The DNA, in turn, passes its genetic instruction to ribonucleic acid (RNA) for directing various metabolic activities of the cell.
a polymer of nucleotides
consists of three parts- a nitrogen base, a deoxyribose, and a phosphate group and makes up DNA
A five-carbon sugar in a nucletotide of DNA
Adenine, Guanine
Double-Ring base (purine)
Thymine, Cytosine
Single-ring base (pyrimidine)
DNA Picture
Differs from DNA in that the sugar that makes up this is Ribose, an thymine is replaced by Uracil, and it is usually single-stranded without forming a double helix
Activation Energy
The sufficient amount of energy the reacting molecules must have after colliding to trigger the formation of new bonds.
Its presence accelerates the rate of the reaction because it lowers the activation energy required for the reaction to take place. It is any substance that accelerates a reaction but does not undergo a chemical change itself. It can be used over and over again.
Chemical reactions that occur in biological systems which includes catabolism, synthesis or anabolism, or the transferring of energy from one substance to another.
The breakdown of substances in a metabolic reaction.
or synthesis, the formation of new products in metabolic reactions
Chemical ____ describesthe condition where the rate of reaction in the forward direction equals the rate in the reverse direction and, as a result, there is no net production of reactants or products.
Globular proteins that act as catalysts (activators or accelerators) for metabolic reactions.
The substance or substances upon which the enzyme acts.
Induced-fit Model
Describes how enzymes work. Within the proten there is an active site with which the reactants readily interact because of the shape, polarity, or other characteristics of the active site. This causes the enzyme to change shape. (Enzymes are also substate specific)
Result of a Reaction with an Enzyme
An enzyme is unchanged as a result of a reaction and it can perform its enxymatic function repeatedly.
Efficiency of an Enzyme
The efficiency of an enzyme is affected by temperature and pH, enzymes lose their ability to catalyze reactions as they become DENATURED and lose their 3-D shape as hydrogen bonds and peptide bonds break down.
Standard suffix for enzymes
nonprotein molecules that assist enzymes.
the union of the cofactor and the enzyme (called an APOENZYME when part of a holoenzyme)
Organic cofactors that usually function to donate or accept some component of a reaction, often electrons. Some vitamins are coenzymes or components of coenzymes.
Inorganic Cofactors
metal ions
Adenosine Triphosphate, a common source of activation energy for metabolic reactions. Itis essentailly an RNA adenine nucleotide with two additional phosphate groups.
The assembly of a new ATP when ADP combines with a phosphate group (Pi) using energy obtainied frmo some energy rich molecule (like glucose)
Picture of ATP
Allosteric Enzymes
These have two kinds of binding sites- one an active site for the substate and one an allosteirc site for an allosteric effector.
Allosteric Effects
An allosteric activator binds to the enzyme and induces the enzyme's ACTIVE form and an allosteric inhibitor binds to the enzyme and induces the enzyme's INACTIVE form.
Feedback Inhibition
Where the end produce or a series of reactions acts as an allosteric inhibitor by shutting down one of the enzymes catalyzing the reaction series.
Competitive Inhibition
When a substance mimics the substrate and inhibits an enzyme by occupying the active site. This mimic displaces the substrate and prevents the enzyme from catalyzing the substrate.
Noncompetitive Inhibitor
This binds to an enzyme at locations other than an active or allosteric site. The inhibitor changes the shape of the enzyme which disables its enzymatic activity.
When an enzyme becomes more receptive to additional substrate molecules after one substate molecule attaches to an active site.