| A | B |
|---|
| Regulation of Protein Function | Alter the synthesis of the protein, Alter rate of degradation of protein, Alter shape or conformation of protein |
| Regulation of Protein Degradation | Proteosomes and Proteins marked for degradation are tagged |
| Proteosomes | large molecular machines that “chew up” proteins; “spit” out pieces/parts |
| Regulation by Shape Modification | Noncovalent interactions and Covalent interactions |
| Protein form | Generated by number of amino acids and kinds of amino acids and largely noncovalent interactions between a. a. |
| General Protein Conformations | Fibrous, Globular, Integral membrane |
| Heirarchical Structure of Proteins | Primary, Secondary, Tertiary, Quarternary |
| Secondary Protein Structures | α helix, β-sheet, β-turn |
| Tertiary Structure | Overall three-dimensional conformation of protein |
| Quarternary Structure | Structure of proteins that consist of multiple polypeptides |
| Motifs | Combination of secondary and tertiary structures |
| Protein Domains | Functional, Structural, Topographical |
| Protein Folding | Amino acid sequence and the properties of a. a. side chains contribute greatly to the “native folding” of a protein |
| Chaperones | facilitate proper protein folding |
| Types of chaperones | Molecular chaperones and Chaperonins |
| Binding! | Specificity and Affinity |
| Enzymes | Biologic catalysts |
