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a life form--a living entity made up of 1 or more cells |
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an explanation for a very general class of phenomena or observations. It is broader in scope than a hypothesis, and it is widely accepted only if there is abundant evidence to support it. |
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a highly organized compartment that is bounded by a thin, flexible structure called a plasma membrane and contains concentrated chemicals in an aqueous solution. |
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all organisms are made from cells, and all cells come from preexisting cells. |
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something that can be measured and that must be correct if a hypothesis is valid |
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a change in the characteristics of a population over time. It means that species are not independent and unchanging entities, but are related to one another and can change through time. |
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the process by which individuals with certain heritable traits tends to produce more surviving offspring than do individuals without those traits, often leading to a change in the genetic makeup of the population. A major mechanism of evolution. |
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refers to traits that can be passed on to offspring. |
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a group of individuals of the same species living in the same area at the same time. |
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changes in populations that occur when HUMANS select certain individuals to produce the most offspring (ie: dog breeding, agriculture) |
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the ability of an individual to produce offspring (high = more surviving offspring) |
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a trait that increases the fitness of an individual in a particular environment |
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the evolution of two or more distinct species from a single ancestral species |
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a family tree of organisms |
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the genealogical relationships of all organisms--literally means "tribe source" |
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cells that have a nucleus, often multicellular organisms, "true kernel" |
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lack a nucleus, often unicellular bacteria and archaea |
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descent with modification |
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early evolutionary/natural selection idea--parents passed on traits to offspring, including heritable traits that increased or decreased fitness. |
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a measure of the ability of an atom to attract electrons toward itself from an atom to which it is bonded. |
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a covalent bond in which electrons are equally shared between atoms of the same or similar electronegativity |
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a covalent bond in which electrons are unequally shared between atoms differing in electronegativity, resulting in the more electronegative atom having a partial negative charge while the other atom(s) have a partial positive charge. |
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a chemical bond that is formed when an electron is completely transferred from one atom to another so that the atoms remain associated due to their opposite electric charges |
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a weak interaction between two molecules or different parts of the same molecule resulting from the attraction between a hydrogen atom with a partial positive charge and another atom (usually O or N) with a partial negative charge |
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interacting readily with water (water loving). Typically polar compounds containing charged or electronegative atoms. |
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not interacting readily with water (water fearing). Typically nonpolar compounds that lack charged or electronegative atoms and often contain many C-C and C-H bonds. |
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the tendency of certain like molecules (e.g. water molecules) to cling together due to attractive forces (hydrogen bonds in water) |
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the tendency of certain dissimilar molecules to cling together due to attractive forces/clinging to surfaces |
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the cohesive force that causes molecules at the surface of a liquid to stick together, thereby resisting deformation of the liquid's surface and minimizing its surface area |
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the amount of energy required to raise the temperature of 1 gram of a substance 1 degree celsius |
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the energy required to change 1 gram of a liquid to a gas |
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the capacity to do work or supply heat. This capacity exists in one of two ways--as stored potential or active motion. |
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stored energy. An object's potential energy is related to its position. |
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the energy of motion. Molecules have kinetic energy because they are constantly in motion. |
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the kinetic energy of molecular motion |
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a measure of how much thermal energy an object's molecules posses. Low temperature = molecules moving slowly, high temperature = molecules moving quickly. |
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thermal energy that is transferred from an object at a higher temperature to one at a lower temperature. |
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first law of thermodynamics |
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energy cannot be created or destroyed, but only transferred and transformed. |
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the amount of disorder in a group of molecules, symbolized by S. |
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second law of thermodynamics |
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entropy always increases in an isolated system (things tend to move toward a lower energy state) |
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the potential energy of the reactants and products, symbolized by H. |
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potential energy of the reactants and products, symbolized by H. |
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Gibbs free energy change (delta G) |
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a measure in the change of potential energy and entropy that occurs in a given chemical reaction. Negative delta G means the reaction is spontaneous. Positive delta G = nonspontaneous. |
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spontaneous reactions, negative delta G |
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nonspontaneous reactions, positive delta G |
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the critically important H-, N-, and O- containing groups found in organic compounds (ie: amino, carbonyl, carboxyl, hydroxyl, phosphate, sulfhydryl) |
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tends to attract a proton and function as a base |
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tends to drop a proton and act as an acid |
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found on aldehyde and ketone molecules such as formaldehyde, acetaldehyde, and acetone. Site of reactions that link these molecules into larger, more complex compounds, like ribose. |
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highly polar, makes compounds more soluble through hydrogen bonding with water; also may act as a weak acid and drop a proton |
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carries two negative charges. When phosphate groups are transferred from one organic compound to another, the change in charge often dramatically affects the recipient molecule (breaking O-P bonds releases a lot of energy). |
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consists of a SH bond. Important in proteins because sulfhydryl groups on different molecules can link together via S-S bonds that contribute to protein structure. |
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protein monomers (building blocks) |
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the act of linking monomers together to form a polymer |
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a macromolecule that consists of amino acid monomers |
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condensation/dehydration reaction |
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monomers polymerize through this--water comes out |
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breaks down polymers--water added |
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the covalent bond between C-N formed by a condensation reaction between two amino acids; links the residues in peptides and proteins |
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chain of many amino acids linked by peptide bonds. Less than fifty = oligopeptide or just a peptide |
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to speed up a reaction (by lowering activation energy) |
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the unique sequence of amino acids in a protein |
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created in part by hydrogen bonding between portions of the peptide-bonded backbone. They are stabilized largely by hydrogen bonding that occurs between the carbonyl oxygren of one amino acid residue and the hydrogen on the amino group of another |
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a form of secondary structure where the backbone is coiled around itself |
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a form of secondary structure where the backbone bends 180 degrees and folds in the same plane |
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results from interactions between R groups or between R groups and the peptide backbone. Types of interactions include hydrogen bonding, hydrophobic interactions, van der Waals interactions, covalent bonding, and ionic bonding |
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hydrogen bonding (tertiary) |
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hydrogen bonds form between hydrogen atoms and the carbonyl group in the peptide-bonded backbone, and between hydrogen and atoms with partial negative charges in side chains. |
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hydrophobic interactions (tertiary) |
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in an aqueous solution, water molecules interact with hydrophilic side chains, forcing hydrophobic side chains to coalesce. When hydrophobic portions of proteins come together, the surrounding water molecules form more hydrogen bonds, increasing their stability. As a result, hydrophobic side chains of proteins tend to form globular masses. |
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van der Waals interactions (tertiary) |
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Once hydrophobic side chains are close to one another, they are stabilized by electrical attractions known as van der Waals interactions. These weak attractions occur because the constant motion of electrons gives molecules a tiny asymmetry in charge that changes with time. A large number of van der Waals interactions can occur in a polypeptide when many hydrophobic residues congregate. The result is a significant increase in stability. |
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covalent bonds (tertiary) |
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form between sulfur atoms when a reaction occurs between the sulfur-containing R groups of two cysteines. Disulfide bonds are frequently referred to as bridges because they create strong links between distinct regions of the same polypeptide. |
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Ionic bonds form between groups that have full and opposing charges. |
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combination of several different polypeptide subunits (ie: hemoglobin molecule with four polypeptide subunits) |
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reactant molecules in a catalysis reaction (reactants) |
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"hump" in graph of energy transfer |
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amount of free energy required to reach the transition state |
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where substrates bind and react/where catalysis usually occurs |
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the enzyme changes shape slightly to tightly bind the substrate to the active site |
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atoms or molecules not part of an enzyme structure that are required for the enzyme to function normally--may be a metal ion or a coenzyme |
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pseudosubstrate blocks substrate from active site |
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allosteric regulation (activation/deactivation) |
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a regulatory molecule changes the shape of the enzyme, either opening up the active site (activation) or closing it off (deactivation) |
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monomers of nucleic acids |
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organic compound with a carbonyl group and several hydroxyl groups |
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