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Unit 2-biochemistry (chapters 5 & 8)
Terms in this set (61)
Subunit or building block molecule of a polymer.
Major structural component of plant cell walls that cannot be digested by most organisms because of missing enzyme.
Another structural polysaccharide found in the exoskeleton of arthropods.
Polymerization reaction during which monomers are covalently linked producing the net removal of a water molecule.
Reaction process that breaks covalent bonds between monomers by the addition of water molecules (requires biological catalysts) (releases energy).
Monosaccharides, disaccharides, polysaccharides.
Single sugars. Store energy in their chemical bonds which is harvested by cellular respiration.
Double sugars. Two monosaccharides joined together.
Hundreds or thousands of monosaccharides.
A type of covalent bond that joins a carbohydrate (sugar) molecule to another group, which may or may not be another carbohydrate.
Glucose polymer in plants stored as granules within plastids.
Glucose polymer in animals stored in skeletal muscles and liver of humans and other vertebrates.
One class of large biological molecules that do not form polymers.
Composed of glycerol and fatty acid.
Three carbon alcohol.
Contains carboxylic acid.
Chemical compounds derived from an acid (organic or inorganic) in which at least one -OH (hydroxyl) group is replaced by an -O-alkyl (alkoxy) group. Usually, esters are derived from a carboxylic acid and an alcohol.
No carbon to carbon double bonds in fatty acids tail.
Carbon skeleton bonded to max number of hydrogens.
Usually solid at room temperature.
Most animal fats.
One or more Carbon carbon double bonds in fatty acid tail.
Tail kinks at each carbon carbon double bond so molecules do not pack enough to solidify.
Usually liquid at room temperature.
Most plant fats.
Composed of glycerol, two fatty acids, a phosphate group.
Composed of four fused carbon rings with various functional groups attached.
Common component of cell membranes. Is precursor to many other steroids.
Polymers of amino acids.
Building blocks of proteins.
What links amino acids together.
Four levels of protein structure
Primary structure, secondary structure, tertiary structure, quaternary structure.
Unique linear sequence of amino acids. Forms the backbone of a protein. Determined by genes. Can be sequenced in the laboratory.
Regular, repeated coiling and folding of proteins polypeptide backbone. Stabilized by H bonds between peptide linkages in proteins back bones.
Irregular contortions of protein due to bonding between sidechains resulting in 3-D shape.
Association of two or more protein subunits to form a single functioning molecule.
Helical coil stabilized by H bonding between every fourth peptide bond.
Sheet of antiparallel chains folded into accordion pleats.
Process that alters the proteins native confirmation and hence it's biological activity.
Store and transmit hereditary information.
Encodes the instructions for amino acid sequences of proteins. Is copied and pasted from one generation of cells to another.
Functions in the actual synthesis of proteins coded for by DNA. Carries the encoded information to the ribosomes; carries the amino acids to the ribosome; a major component of ribosomes.
Polymers of monomers.
How nucleotides are joined together. Between phosphate of one nucleotide and the sugar of the next.
Two of the five bases in nucleic acid A in G.
Two of the five bases. T and C.
The totality of an organisms chemical reactions.
Releases energy by breaking down complex molecules into simpler compounds.
Consumes energy to build complex molecules from simpler ones.
Energy associated with motion.
Energy that matter possesses because of its location or structure.
Absorbs free energy from its surroundings and it's nonspontaneous.
Proceeds with the net release of free energy and is spontaneous.
The initial energy needed to start a chemical reaction.
Chemical agent that speeds up or reaction without being consumed by the reaction.
Speed up metabolic reactions by lowering energy barriers.
The reactant that on enzyme acts on.
Region of an enzyme which binds to the substrate. Is usually a pocket or groove on surface. Determines enzyme specificity.
The change in the shape of an enzymes active site which is induced by the substrate.
Small nonprotein molecules required for proper enzyme function. May bind to active site or substrate.
Chemicals that resemble an enzymes normal substrate and complete with it for the active site. Block active site from substrate.
Enzyme inhibitors the do not enter the active site but bind to another part of the enzyme molecule. Cause enzymes to change its shape so active site cannot find substrate. May act as a metabolic poison.
A form of allosteric regulation that can amplify enzyme activity. By binding by a substrate to one active site stabilizes favorable confirmational changes at all other subunits.
The term used to describe cases where proteins function at one site is affected by binding of a regulatory molecule at another site.
The place on an enzyme where a molecule that is not the substrate may bind best changing the shape of the enzyme and influencing its ability to be active.
The end product of a metabolic pathway shuts down the pathway that produced it. Prevents the cell from wasting chemical resources by synthesizing more product than is needed.
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