Exam I Vocabulary B Flashcards
Primary Protein Structure
amino acid sequence
Secondary Protein Structure
local structure; alpha helices and beta sheets
Tertiary Protein Structure
folded structure of the entire polypeptide chain
Quaternary Protein Structure
arrangement of multiple subunits into a larger complex
Homodimer
two copies of the same protein which bind together
Heterodimer
two different proteins which bind together
Alpha Helix
hydrogen bonds
Alpha Helix
hydrogen bonds and pi stacking aromatic molecules; certain; often transmembrane part of a protein
Beta Sheet
can let a protein interact with two different kinds of regions because it’s double sided; two or more chains of amino acids; can be antiparallel or parallel
Antibody
binds antigens very specifically; in some cases, antibody can distinguish between proteins that differ by a single amino acid
Antigen
foreign substance that elicits production of an antibody
Heavy Chain
larger part of the antibody
Light Chain
smaller part of the antibody
Enzyme
speed up reactions by factors of 10^6 or more;
Catalyst
lower the activation energy by interacting with transition state (free energy of substrates and products remain the same)
Enzyme
speed up reactions by factors of 10^6 or more; usually has “-ase” at the end; lowers activation energy of a reaction
Enzyme
speed up reactions by factors of 10^6 or more; usually has “-ase” at the end; lowers activation energy of a reaction; facilitate orientation of substrates, change reactivity of substrates, induce strain on substrates
Substrate
a molecule that undergoes an enzyme-catalyzed reaction; becomes a product after reacting with an enzyme
Product
differs from substrates by one or more covalent bonds
Activation Energy
the difference between the energy of the reactants and the energy of the transition state; must be overcome for the reaction to occur; lowered by the catalyst
Allosteric Regulation
conformation of enzyme changes shape upon binding a regulatory molecule (ligand); binds somewhere other than the active site and induce a conformational change that affects the substrate binding to the active site
Competitive Inhibition
block substrates from binding to the active site
Ion Exchange Chromatography
separates proteins by charge; charged beads attract a proteins of a certain charge, while the other ones move through the column more quickly
Gel Filtration Chromatography
separates proteins by size; small molecules enter aqueous spaces within beads