Cell Membranes and Signalling Flashcards
state what it is meant by the key term - ligand
a ligand is any molecule, or ion, that is bound to a protein by electrical attractions or hydrophobic forces
state, and explain, the two forces in which ligands can be bound to proteins
- electrical attractions between oppositely charged ionic or polarised groups on the ligand and protein
- weaker attraction due to hydrophobic forces between non polar forces on the two molecules
state, and explain, what it is meant by the key term - binding site (4 points)
- the point on the protein which the ligand binds to
- not covalent + easily reversible
- binding causes a conformational change in the shape of the protein
- then proteins specific function is then activated/inactivated
state what it is meant by the key term - chemical specificity
the ability of a protein binding site to bind specific ligands (in order to bind correctly, they must have a complementary shape)
state 2 facts about binding sites
- conformation determined by sequence of amino acids in the primary protein structure
- some binding sites are only complementary in shape / specific to one ligand, and some to several
state what it is meant by the key term - affinity
the strength of a ligand-protein binding - affinity determines how easily binding occurs and releases
state the definitions for the three type of binding in relation to affinity
- strong binding - site containing a positively charged amino acid side chain
- less strong bonding - a site which has the same shape but not a positively charged amino acid side chain
- weaker bonding - different shape and no positively charged amino acid side chain
state what it is meant by the key term - saturation
the percentage total ligand binding sites that are occupied at one point in time
state the two determinants of percentage saturation
- concentration of unbound ligands in solution
2. ligand affinity to ligand binding site
state the two ways to control protein activity
- change the protein shape - alters ligand binding ability
2. regulating protein synthesis and degradation
there are two mechanisms in cells which can selectively alter protein shape. name these two mechanisms
- allosteric modulation
2. covalent modulation
state what it is meant by the key term - allosteric modulation
occurs when a protein has two binding sites and the binding of a protein to one of the binding sites alters the shape of the other binding site
state the names of the two binding sites on a protein (allosteric modulation)
- functional/active site - carries out the proteins physiological functions
- regulatory site
state what it is meant by the key term - modulator molecules (allosteric modulation)
modulator molecules are ligands that bind to regulatory sites. it’s binding modulates the shape, and therefore activity, of the active site/functional unit of the protein
state what it is meant by the key term - cooperativity
when a ligand binds to the first of several active/functional sites on a molecule and induces a change that increases the affinity of the other active/functional sites
state what it is meant by the key term - covalent modulation
the covalent bonding of charged chemical groups to some of the protein side groups
explain what kinase and phosphatase is (covalent modulation)
- kinase - an enzyme that adds a phosphate group to another molecule
- phosphatase - an enzyme that removes the phosphate group from another molecule
metabolism consists of two aspects. state and explain these two aspects
- anabolism - the synthesis of organic molecules
2. catabolism - the breakdown of organic molecules
state what it is meant by the key term - 1 calorie
1 calorie = the amount of heat required to raise the temperature of 1 g of water by 1’c