Totality of an organism's chemical reactions. Interactions between molecules within cells.
Pathways release energy by breaking down complex molecules into simpler compounds.
Consume energy to build complex molecules from simpler ones.
Capacity to cause change.
Energy associated with motion.
Kinetic energy associated with random movement of atoms or molecules.
Energy that matter possesses because of its location or structure
Potential (stored) energy available for release in a chemical reaction.
Isolated from its surroundings.
Energy and matter can be transferred between the system and its surroundings.
Proceeds with a net release of free energy and its spontaneous.
Absorbs free energy from its surrounding and is nonspontaneous.
Subunit or building block molecule of a polymer.
Large molecule consisting of many identical or similar subunits connected together.
Large organic polymer (Ex. Carbs, lipids, proteins, nucleic acid)
Polymerization reaction during monomers are covalently linked, producing a net removal of a water molecule for each covalent linkage.
Reaction process that breaks covalent bonds between monomers by the addition of water molecules.
Single sugars. Major nutrients in cells, store energy in their chemical bonds. Fuel for cells.
Most common monosaccride
Molecular formula of monosaccharides
2 monosaccharides formed when a dehydration reaction joins two monosaccharides. Glycosidic linkage.
Hundreds of thousands of monosaccharides.Held together by Glycosidic linkage. Have storage and structural roles. Structure and function determined by sugar monomers and position of linkages.
Glucose polymer in plants stored as granules within plastids.
Glucose polymer in animals stored in skeletal muscles and liver of humans and other vertebrates.
Major structural component of plant cell walls that cannot be digested by most organisms because of missing enzyme. Insoluble fiber.
Structural polysaccharide found in exoskeleton of anthropods, cell walls of fungi, and surgical thread.
Do not form polymers. They are hydrophobic. Nonpolar covalent bonds. Fats, phospholipds, steroids.
Composed of glycerol and fatty acid. Contains Ester linkages
Contains carboxyl acid, long hydrocarbon chain or "tail". The nonpolar C-H bonds make the chain hydrophobic and insoluble in water.
Bond between a hydroxyl/carboxyl group. Bond in lipids.
No c-c double bond in fatty acid tail, carbon skeleton bonded to max # of hydrogen, Solid at room temperature.
One or more c-c double bonds in fatty acid tail, tail kinks at c-c so molecules do not pack closely together and are liquid at room temperature.
Functions of Fat
Energy storage, cushions vital organs in mammals, insulates against heat loss.
Composed of glycerol, 2 fatty acids, a phosphate group.
Composed of 4 fused carbon rings w/ various functional groups attached. Hydrophobic.
Precursor to many other steroids (including sex hormones in vertebrates) Common component of cell membranes. Can cause atherosclerosis
Speeds up metabolic reactions by lowering energy barriers. Catalytic protein.
Chemical agent that speeds up a reaction without being consumed by the reaction.
Name of the covalent bond that links 2 amino acids together. Requires dehydration.
50% of dry mass of cells.
Consist of 1 or more polypeptide chains folded and coiled into specific conformations.
Polymers of amino acids. Arranged in specific linear sequence. Linked by peptide bonds.
Building blocks of proteins
Structure of Amino Acid
Central carbon, hydrogen atom, carboxyl group, amino group, variable R group
Unique, linear sequence of amino acids. Determined by genes.
Regular, repeating coiling and folding of proteins polypeptides backbone. Stabilized by H-bonds between peptide linkages in protein's backbone.
Helical coil stabilized by H-bonding between every fourth peptide bond.
Beta Pleated Sheet
Sheet of antiparallel chains folded into "accordion" pleats.
Irregular contortions of protein due to bnding between side chains (R group) resulting in 3-D shape.
Association of 2 or more protein subunits to form a single functioning molecule (i.e. hemoglobin and collagen)
Process that alters a protein's native conformation and hence its biological activity. Heat, salt concentration, chemical agents, pH changes, transfer to organic solvent)
Store and transmit hereditary information
Amino acid sequence of a polypeptide is programmed by a unit of inheritence called a....
Genes are made of...
Directs synthesis of messenger RNA and through mRNA controls protein synthesis
Protein synthesis occurs in...
Encodes the instructions fro amino acid sequence in proteins, copied and passed out from one generation of calls to another.
Functions in the actual synthesis of proteins copied by DNA, carries encoded information to the ribosomes. Carries the amino acids to the ribosomes.
Polymers of monomers. Consist of Pentose, Phosphate group, and nitrogenous base.
Nucleotides are joined together by...
Guanine bonds with
Thymine bonds with
6 membered ring fused to 5 membered ring. Adenine and Guanine
Six membered ring of carbon and nitrogen atoms. Cytosine, thymine, and uracil.
Initial energy needed to start a chemical reaction
Region of an enzyme which binds to the substrate .Determines enzyme's specificity.
The reactant that an enzyme acts
a change in shape of an enzyme;s active site which is induced by the substrate. Enhances ability to catalyze reactions.
Small non-protein molecules required fr proper enzyme function.
Organic cofactors .
Chemicals that resemble an enzyme's normal substrate and compete with it for the active site.
Do not enter substrate but bind to another part of the enzyme.
Cases where protein's function at one site is affected by binding to a regulatory molecule at another. May inhibit or stimulate enzyme's activity.
end product of a metabolic pathway shuts down the pathway that produced it.