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ODSC 6B
| Question | Answer |
|---|---|
| I. Protein overview | |
| Protein | a series of amino acids linked together by covalent peptide bonds |
| Peptide bond | special covalent that can be broken with strong acid or base at High Temp |
| Characteristics 3 | No rotation(partial double bond), trans config, uncharged but polar |
| More Characteristics | neither accept or give off protons and participate in H bonding |
| Sequences Amino Acid | |
| Can determine Amino Acid Composition by | |
| 1. acid hydrolysis which | cleaves all peptide bonds |
| 2. Cation exchange chromatography | which separates aa |
| 3. Quantitative analysis | using spectroscopy |
| Edmans reagen | individually cleaves the aa from N |
| Enzymatic cleavage | specific enzymes cleave a , specific regions |
| Multimeric proteins | a protein with more than one polypeptide |
| II. Structure | |
| 5 categories of proteins | primary, seconday, tertiary, quaternary |
| 1. Primary structure | linear sequence of aa |
| 2. Secondary structure | thre dimensional arrangements alpha helices, beta sheets |
| Alpha helix | extensive H bonds, H bonds to NH group, 3.6 aa per turn |
| Disrupted by | proline, charged aa, and typtophan with bulky side chain |
| Beta Sheet | appears pleated with H bonds between chains |
| Beta Sheets can be | parallel or antiparallel |
| Amloid protein | fibrous protein composed of beta sheeets |
| Beta bends | revers the direction of a polypeptide chain and usually connect successive strands of antiparallel sheets |
| Beta sheets are composed mostly of | proline and glycine |
| Non repetitive secondary structure | do not fall into Alpha or Beta category |
| Supersecondary structures | motifs of combination of secondary structures, ex; beta alpha beta |
| 3. Tertiary structure | combination of secondary structures and motifs forming domains. 3D structure |
| Domains | fundamental functional unit that is made of supersecondary structures |
| 4. Quaternary structure | polypeptide subunits are arranged and held together by noncovalent interactions |
| III. Interactions | |
| Chaperones | specialized group of proteins that aid in the folding of proteins during translation |
| Stabilizing Interactions | |
| 1. Disulfide bonds | covalent linkage of sulfhydryl group of to mol |
| 2. Hydrophobic interactions | non polar side chains are located in the inner of the protien |
| 3. Hydrogen Bonds | side chains such as OH or NH can form H bonds |
| 4. Ionic Interactions | neg and pos groups stabilize protein |
| IV. Denaturation | |
| Denaturation | unfolding and disorganization, may never turn back |
| Caused by | heat, acids, base, detergents |
| V. Disease | |
| Prion causes many different diseases | transmissible spongiform encephalopathies, creutzfeld jakob, scrapie, mad cow |
| Caused by | alpha helix turning into beta sheet |
Created by:
mcap
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