Ch 4 - Protein Structure and Function Flashcards
active site
region on the surface of an enzyme that binds to a substrate molecule and catalyzes its chemical transformation
allosteric
describes a protein that can exist in multiple conformations depending on the binding of a molecule (ligand) at a site other than the catalytic site; such changes from one conformation to another often alter the protein’s activity or ligand affinity
α helix (alpha helix)
folding pattern, common in many proteins, in which a single polypeptide chain twists around itself to form a rigid cylinder stabilized by hydrogen bonds between every fourth amino acid
amino acid sequence
the order of the amino acid subunits in a protein chain. sometimes called the primary structure of a protein
antibody
protein produced by B lymphocytes in response to a foreign molecule or invading organism. binds to the foreign molecule or cell extremely tightly, thereby inactivating it or marking it for destruction
antigen
molecule or fragment of a molecule that is recognized by an antibody
β sheet (beta sheet)
folding pattern found in many proteins in which neighbouring regions of the polypeptide chain associate side-by-side with each other through hydrogen bonds to give a rigid flattened structure
binding site
region on the surface of a protein, typically a cavity or groove, that interacts with another molecule (a ligand) through the formation of multiple noncovalent bonds
C-terminus
the end of a polypeptide chain that carries a free carboxyl group (-COOH)
chromatography
technique used to separate the individual molecules in a complex mixture on the basis of their size, charge, or their ability to bind to a particular chemical group. in a common form of the technique, the mixture is run through a column filled with a material that binds the desired molecule, and it is then eluted from the column with a solvent gradient.
coenzyme
small molecule that binds tightly to an enzyme and helps it to catalyze a reaction
coiled-coil
stable, rodlike protein structure formed when two or more α helices twist repeatedly around each other
conformation
precise, three-dimensional shape of a protein or other macromolecule based on the spatial location of its atoms in relation to one another
cryoelectron microscopy (cryo-EM)
technique for observing the detailed structure of a macromolecule at very low temperatures after freezing native structures in ice
disulfide bond
covalent cross-link formed between the sulfhydryl groups on two cysteine side chains; often used to reinforce a secreted protein’s structure or to join two different proteins together
electrophoresis
technique for separating a mixture of proteins or DNA fragments by placing them on a polymer gel and subjecting them to an electric field. the molecules migrate through the gel at different speeds depending on their size and net charge
enzyme
a protein that catalyzes a specific chemical reaction
feedback inhibition
a form of metabolic control in which the end product of a chain of enzymatic reactions reduces the activity of an enzyme early in the pathway
fibrous protein
a protein with an elongated, rodlike shape, such as collagen or a keratin filament
globular protein
any protein in which the polypeptide folds into a compact, rounded shape. includes most enzymes