BioE 220 Chapter 4

The addition of one or more acetyl groups to a protein; the formation of an acetyl derivative

The input of energy required to initiate a chemical reaction. Enzymes increase rate of reaction

The region of an enzyme that binds substrates and catalyzes an enzymatic reaction

The addition of one or more acyl groups to a protein

A measure of the degree to which a substance tends to bind to another

A common secondary structure of proteins in which the linear sequence of amino acids is folded into a right-handed spiral stabilized by hydrogen bonds between carboxyl and amide groups in the backbone; a coiled secondary structure of a polypeptide chain formed by hydrogen bonding between amino acids separated by four residues.

A specialized immune protein, which helps fight infection by neutralizing pathogens and tagging them for destruction

A planar secondary structure of proteins that is created by hydrogen bonding between the backbone atoms in two different polypeptide chains or segments of a single folded chain; a sheetlike secondary structure of a polypeptide chain, formed by hydrogen bonding between amino acids located in different regions of the polypeptide. 

A substance that increases the rate of a reaction without itself undergoing any chemical change

A compound formed by two molecules of a simpler compound; a polymer formed from two molecules of a monomer

A covalent linkage formed between two sulfhydryl groups on cysteines. Joins two proteins together or linking different parts of the same protien.

A biological substance produced by living organisms to increase the rate of a biochemical reaction

The addition of one or more sugars to  protein or lipid molecule

The tendency of nonpolar groups to cluster so as to shield themselves from contact with an aqueous environment

A transmembrane protein that transports ions, which are otherwise impermeable to the cells

Any molecule that binds tightly and specifically to a macromolecule, usually a protein, forming a ma romolecule-ligand complex

A graphical model used to determine the maximum reaction rate, V_max and Michaelis constant, K_m. 

The value equal to the substrate concentration at which the enzyme reaction proceeds at half of the max velocity

Describes the velocity of a given reaction developed from a simple model of enzyme substrate kinetics

The addition of myristic acid to the N-terminal glycine residue of a polypeptide chain

Proteins that have not yet achieved their functional final folding pattern

A covalent bond that links adjacent amino acid residues in proteins; formed by a condensation reaction between the amino group of one amino acid and the carboxyl group of another with the release of a water molecule

A reaction in which a phosphate group becomes covalently coupled to another molecule

The enzyme-catalyzed change to a protein made after it is synthesized

An enzyme such as trypsin that degrades proteins by hydrolyzing some of their peptide bonds

A substance that functions by inhibiting the actions of a protease

The degradation of polypeptide chains

The complete set of proteins present in the cell

A branch of molecular biology concerned with determining the proteome

A transmembrane protein that has an extracellular domain that binds to molecules called ligands

The comparison of an unknown primary amino acid sequence to a database of known primary amino acid sequences in an attempt to identify functional capabilities of the unknown amino acid

The molecule on which an enzyme acts

The structure that forms transiently in the course of a chemical reaction and has the highest free energy of any reaction intermediate. 

A rate constant that is equal to the number of substrate molecules processed per enzyme molecule each second

A technique for determining the 3-D structure of macromolecules by passing x-rays through a crystal of the purified molecules and analyzing the diffraction pattern of x-rays is used to determine the arrangement of individual atoms within a molecule