isomers that are mirror images of each other; cannot be rearranged because of bonding or shape
important chemical groups that affect a molecule's shape and the chemical reactions of a molecule
an isomer in which there are identical covalent partnerships, but they differ in spatial arrangements; differences arise from flexibility of single bonds
organic molecules consisting only of carbon and hydrogen; atoms of hydrogen are attached to the carbon skeleton wherever electrons are available; not present in living organisms, but cells' organic molecules have regions that contain these
compounds that have the same numbers of atoms of the same elements but different structures and therefore different properties
the view that physical and chemical laws govern all natural phenomena, including the processes of life
the branch of chemistry that specializes in the study of carbon compounds
an isomer in which there are different covalent arrangements of atoms; location of double bonds can differ
the belief in a life force outside the jurisdiction of physical and chemical laws
a secondary structure that is a delicate coil held together by hydrogen bonding between every fourth amino acid
organic molecules possessing both carboxyl and amino groups
beta pleated sheet
a secondary structure in which two or more regions of the polypeptide chain lying side by side are connected by hydrogen bonds between parts of two parallel polypeptide backbones; it makes up the core of globular proteins
a sugar (monosaccharide) or one of its dimers (disaccharides) or polymers (polysaccharides)
a polysaccharide that is a major component of the tough walls that enclose plant cells; most abundant organic compound on Earth; polymer of glucose
protein molecules that assist in the proper folding of other proteins; they do not specify the final structure of a protein, instead they keep the new polypeptide separated from "bad influences" in the cytoplasmic environment while it folds
an important structural polysaccharide used by arthropods to build their exoskeletons; pure forms of this are leathery and flexible, but they harden when encased within calcium carbonate
a common component of animal cell membranes, and a foundation from which other steroids are synthesized; crucial molecule in animals, but can be dangerous when in high amounts
when two monomers connect to each other by a reaction in which two molecules are covalently bonded to each other through a loss of a molecule
contractile and motor
the type of protein that controls movement; example: actin and myosin are responsible for the contraction of muscles; other proteins are responsible for the undulations of cilia and flagella
the type of protein that protects against disease; example: antibodies combat bacteria and viruses
when two monomers connect to each other by a reaction in which a hydroxyl group covalently bonds to a hydrogen atom, which causes the loss of a water molecule in the process
the unraveling and loss of a protein's native shape due to alterations of its environment, such as pH, salt concentration, and temperature; this causes a protein to become biologically inactive
a double-stranded, helical nucleic acid molecule consisting of nucleotide monomers with a deoxyribose sugar and the nitrogenous bases adenine, guanine, cytosine, and thymine; it is capable of replicating and determining the inherited structure of a cell's proteins
the sugar connected to DNA; has one less oxygen atom than the other sugar associated with nucleic acids
molecule that consists of two monosaccharides joined by a glycosidic linkage
links that form where two cysteine monomers are brought together by folding of protein; covalent bonds reinforce structure
the shape that cellular DNA molecules take as a result of spiraling around an imaginary axis; this was proposed by James Watson and Francis Crick in 1953 at Cambridge University
the type of protein that selectively accelerates chemical reactions; example: digestive enzymes release polymers in food
specialized macromolecules that speed up chemical reactions in cells; considered proteins
a large molecule constructed by two smaller molecules, glycerol and a fatty acid, through dehydration reaction; major function is energy storage
a molecule with a long carbon skeleton (usually 16 or 18 in length) and a carboxyl group at the end of the molecule (hence the acid); these are hydrophobic
the shape of proteins that are long and fiber-like
a discrete unit of hereditary information consisting of a specific nucleotide sequence in DNA (or RNA, in some viruses)
the shape of proteins that are roughly spherical
an alcohol with three carbons, each having a hydroxyl group
a polymer of glucose that is like amylopectin (a complex starch that is a branched polymer with 1-6 linkages at branch points) but more extensively branched; animals store this
a covalent bond formed between two monosaccharides by a dehydration reaction; the most common type of this in nature is a "1-4"
the type of protein that coordinates an organism's activities; example: insulin, a hormone secreted by the pancreas, helps regulate the concentration of sugar in the blood of vertebrates
a process that occurs when the bonds between two monomers are broken by the addition of water molecules, with a hydrogen from the water attaching to one monomer and a hydroxyl group attaching to the adjacent monomer
an interaction that contributes to tertiary structure; as a polypeptide folds into functional shape, amino acids with hydrophobic side chains usually end up in clusters at the core of the protein, away from water
one of a group of compounds, including fats, phospholipids, and steroids, that mix poorly, if at all, with water; they are not composed of true polymers, so they are generally not large enough to be considered macromolecules; they are hydrophobic because they contain few polar bonds and many hydrocarbon regions; they vary in form and function
giant molecules formed by the joining of smaller molecules, usually by a condensation reaction; polysaccharides, proteins, and nucleic acids are considered these
a nucleic acid that directs the production of polypeptides; this is found in the cells' ribosomes
repeating units that serve as building blocks of a polymer; smaller molecules; some also have functions on their own
molecules with a general formula of some multiple of the unit CH2O; these are major nutrients as carbon skeletons serve as raw material for synthesis of other organic molecules
a polymer (polynucleotide) consisting of many nucleotide monomers; serves as a blueprint for proteins, and through the actions of proteins, for all cellular activities; two types are DNA and RNA
the monomer of nucleic acids that has three parts: 1) a nitrogenous base (A, C, G, T, U); 2) a give-carbon sugar (a pentose); 3) a phosphate group
a covalent bond that results when two amino acids join through dehydration reaction
cells need these in order to exist because they make up cell membranes; has 2 fatty acids attached to glycerol instead of traditional 3 (triacylglycerol); always assemble into a double-layer aggregate because of hydrophilic head and hydrophobic tail
a long molecule consisting of many similar or identical building blocks linked by covalent bonds, much as a train consists of a train of cars; carbohydrates, nucleic acids, and proteins are examples of these
polymers of all amino acids
macromolecules; polymers with a few hundred to a few thousand monosaccharides joined by glycosidic linkages; serve as storage material, hydrolyzed as needed to provide sugar for cells; building material for structures that protect a cell or an organism; architecture and function are determined by sugar monomers and by positions of glycosidic linkages
the unique structure of amino acids; example: a polypeptide composed of 127 amino acids has 20^127 different ways it can be organized
macromolecules that are constructed from one or more polypeptides, each folded and coiled into a specific three-dimensional structure; all made from same 20 amino acids; most structurally sophisticated molecule known
the family of larger nitrogenous bases in which its members have a six-membered ring fused to a five-membered ring; members are adenine (A) and guanine (G)
the family of smaller nitrogenous bases in which its members have six-membered rings of carbon and nitrogen atoms; members include cytosine (C), thymine (T), and uracil (U)
the overall protein structure that results from the gathering of polypeptide subunits; some proteins consist of 2 or more polypeptide chains combined into one macromolecule
the type of protein that helps a cell respond to chemical stimuli; example: receptors built into the membrane of a nerve cell detect chemical signals released by other nerve cells
a type of nucleic acid consisting of nucleotide monomers with a ribose sugar and nitrogenous bases adenine, cytosine, guanine, and uracil; usually single-stranded; functions in protein synthesis, gene regulation, and as the genome of some viruses
the sugar connected to RNA; has one more oxygen atom than the other sugar associated with nucleicacids
a fat made from saturated fatty acid; animal fats are solid at room temperature because they lack double-bonds, thus flexibility enables molecules to pack together tightly
saturated fatty acid
a fatty acid that has no double-bonded carbon atoms so that as many hydrogen atoms as possible are bonded to the carbon skeleton
the collection of coils and folds that result from hydrogen bonds between repeating constituents of the polypeptide backbone (not the amino acid sides)
an inherited blood disorder that is caused by a substitution of one amino acid (valine) for the normal amino acid (glutamic acid) at a particular position in the primary structure of hemoglobin, the protein that carries oxygen in red blood cells
a polymer of glucose monomers; synthesizing this allows for the storage of glucose, and thus, stored energy; this molecule is helical in shapeq
lipids characterized by a carbon skeleton consisting of four fused rings
the type of protein that stores amino acids; example: ovalbumin is the protein of egg white, used as an amino acid source for developing embryos
the type of protein that supports an organism; example: insects and spiders use silk fibers for cocoons and webs, collagen and elastin provide fibrous framework in animal connective tissues; keratin is protein of hair, horns, feathers, etc.
the overall shape of a polypeptide that results from interactions between side chains of various amino acids
the fat that results when unsaturated fats are synthetically converted to saturated fats to prevent the separation of lipids (margarine and peanut butter are examples); this process produces saturated fats and unsaturated fats with trans double bonds
the type of protein that transports other substances; example: hemoglobin, the iron-containing protein of vertebrate blood, transports oxygen from lungs to other parts of the body
a fat that consists of three fatty acids linked to one glycerol molecule; linkages that bond hydroxyl to carboxyl are called ester linkages
a fat made from unsaturated fatty acids; they are liquid at room temperature (oils) because kinks in -cis bonding prevent molecules from packing together to solidify
unsaturated fatty acid
a fatty acid that has one or more double-bonded carbon atoms formed by the removal of hydrogen atoms from the carbon skeleton; there will be a kink in the hydrocarbon chain wherever a -cis double-bond occurs (causes bending)
the method used to determine 3-D structures of proteins; developed in 1959
a functional group consisting of a hydrogen atom bonded to an oxygen atom by a polar covalent bond(—OH), which in turn is bonded to the carbon skeleton of a molecule. Molecules possessing this group are water soluble and called alcohols.
organic compounds containing hydroxyl groups.
a functional group present in aldehydes and ketones consisting of an oxygen atom double bonded to a carbon atom.
Name of carbonyl compound when it is within the C-skeleton
an organic molecule with a carbonyl group at the end (terminal) of the carbon skeleton.
a functional group present in organic acids consisting of a carbon atom double-bonded to an oxygen and also bonded to a hydroxyl group.(—COOH)
organic acids; compounds containing a carboxyl group.
(—NH2) a functional group composed of nitrogen atom bonded to two hydrogen atoms and to the carbon skeleton. Can act as a base in solution, accepting a hydrogen ion and acquiring a charge of +1.
organic compound with one or more amino groups.
(—SH) a functional group consisting of a sulfur atom bonded to a hydrogen atom.
organic compound containing sulfahydryl groups.
a functional group consisting of a phosphorus atom covalently bonded to four oxygen atoms and is important in energy transfer.
polysaccharides of thousands of glucoses; store energy; allows organisms to store thousands of glucoses in 1 polysaccharide molecule. The glycogen breaks down glucose in the digestive tract, and is synthesized from glucose in the liver
Spatial location of the atoms of a molecule. The precise shape of a protein or other macromolecule in three dimensions.
A class of enzymes that help proteins fold into the correct configuration and can refold proteins that have been misfolded or denatured
A polymer consisting of many nucleotide monomers; serves as a blueprint for proteins and, through the actions of proteins, for all cellular activities. The two types are DNA and RNA