Lehninger Ch 5 Flashcards
Ligand
A small water-insoluble biomolecule generally containing fatty acids, sterols, or isopreniod compounds (a ligand is a protein)
Binding site
The crevice or pocket on a protein in which the ligand binds
Induced fit
An enzyme conformation change in response to substrate binding that renders the enzyme catalytically active; also denotes a conformation change in any macromolecule in response to ligand binding, such that the binding site better conforms to the shape of the ligand
Hemoglobin
A heme protein in erythrocytes; functions in oxygen transport
Heme
The iron-porphyrin prosthetic group of heme proteins
Porphyrin
A complex nitrogenous compound containing four substituted pyrroles covalently joined in a ring; often complexed with a central metal atom
Globins
Are a widespread family of oxygen-binding proteins. Commonly found in eukaryotes of all classes, as well as in archea and bacteria. All evolved from a common ancestral protein. Their tertiary structure is highly conserved, made up of eight a-helical segments connected by bends
Globin fold
Their tertiary structure is highly conserved, made up of eight a-helical segments connected by bends. This folding pattern, illustrated by myoglobin constitutes a structural motif known as the globin fold
Equilibrium expression
The reversible binding of a protein (P) to a ligand (L)
Association constant, Ka
Describes the equilibrium between the complex and the unbound components of the complex. The association constant provides a measure of affinity of the Ligand
Dissociation constant, Kd
The reverse of the association constant, high Ka means low Kd
The reciprocal of Ka and has units of molar concentration (M)
Allosteric protein
An allosteric protein is one in which binding of a ligand to one site affects the binding properties of another site on the same protein ex hemoglobin is in T state becomes more R state the more oxygen binds
Modulator
Allosteric proteins are those having “other shapes” or conformations, induced by the binding of ligands referred to as modulators. The conformation changes induced by the modulator(s) interconvert more-active and less-active forms of the protein
Homotrophic
When the normal ligand and the modulator are identical, the interaction is termed homotrophic
Heterotrophic
When the modulator is a molecule other than the normal ligand.