A ligand is a
Molecule that binds to a protein
Disulfide Bond
Covalent bond between 2 cystines in a protein
Peptide bond
Covalent bond linking the amino group of one amino acid to the carboxyl group of another amino acid
Almost all cellular processes are carried out by
Proteins
Defense, transport, and structure
Antibodies, sodium potassium pump, keratin
Function of Ribsomes
Synthesizes proteins
Alpha-Helix is an example of—— and is held together by——
Secondary, hydrogen bonds
Proteins must be—-to work
Certain shape
Central Carbon
Attaches amino, phosphate, and side chain groups
If a molecule binds to a protein—
The shape of the protein changes
If a protein unfolds due to change in pH
Denaturation
Asn and Ser interaction
Hydrogen bond
Lys and Asp interaction
Ionic bond
Enzymes
Are extremely specific
Allosteric inhibition
Inhibition by a binding event at a site different from the active site, inducing a shape change and reduces the enzyme’s affinity for its substrate
Allosteric activator repeat sorry
Binds to locations away from the active site, inducing a conformational change that inc. affinity of enzyme’s active site for its substrate.
Catabolic reaction
Releases energy, by breaking larger molecules down into smaller molecules
Anabolic reaction
Requires energy, by building smaller molecules into larger molecules
Cofactors
Inorganic ion such as a mineral required for optimal enzyme activity regulation
Coenzymes
Small organic molecule, such as vitamins or its derivative, which is required to enhance an enzymes activity.
Competitive inhibition
Inhibitor competes with the substrate molecule by binding to the active site (reversible)
Denature
Loss of shape in a protein; can happen as a result of changes in temperature, pH, or chemical exposure
Feedback inhibition
When an enzyme is inhibited by the end product of a pathway in which it is involved
Primary level of stucture
Linear sequence of amino acids in a protein