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Proteins
Biosci 106
| Question | Answer |
|---|---|
| Basic structure of an Amino Acid? | -COOH (carboxyl grp) -NH2 (amino group) -central alpha C -side chain R |
| Important properties on AA? | -zwitterion when neutral -sterioisomer are Alpha C |
| AA zwitterion | -When Nuetral -Protonated NH3+ -dissociated -OH |
| what form of sterioisomers of AA are only found in protiens? | -L-isomers -NOT D |
| # of AA? | -20 AA -R side group changes |
| non-polar side chain AA -example | -R = C+H mostly -hydrophobic -glycine, Proline |
| Polar side chain -Example | -hydrophillic -R= -OH -COONH2 -form hydrogen bonds -cysteine (SH) |
| Basic AA | -hydrophillic -+vely charged -lysine, histidine, arginine |
| Acidic AA | -hydrophillic --vely charged -glutamic acid, aspartic acid |
| pH below pKa? | Basic +ve protonated |
| pH above pKa? | -ve non-protonated acidic |
| secondary structure | Alpha helix Beta sheets regular and repetitive formed by polypeptide backbone |
| Alpha Helix | 3.6AA/turn R groups poke out bulky Clock-wise R-hand coil |
| Beta sheet | strands run anti/parallel flexible, roll-up,twist R-group point up/down |
| Metlittin | Alpha helix W kink 26AA active component of bee-sting |
| Proline | no NH2 side group can't H bond |
| Fibrous protein | used for strength collagen, keratin repetitive |
| Alpha Keratin | coil with globular head cysteine forms disulphide bond amphipathic |
| Fibroin | Beta sheets forms layers- alternating;gly,ala,ser |
| Collagen | special helices no H-bonding triple helix |
| glycosylation | addition of sugars to chain |
| phosphorylation | phosphate added |
| Globular protein features | Alpha,Beta or irregular loops tertiary structure hydrophobic-inside Hydrophillic-outside structure determined by -R |
| Domains of globular protein | 100-300 residues seperately folded regions different activities occur |
| Globular proteins -interactions | hydrophobic hydrogen bonding ion pairs disulphide |
| Hydrogen bonding | form backbone H- of residues poking out |
| Hydrophobic interactions | hide on inside driving force of folding |
| Ionic pairs | NH+--OOC charge depends on pH |
| Disulphide bond | doesn't cause folding happens when cysteine comes close |
| Denaturation | ph Temperature organic solvent detergent |
| Protein folding | initiated- H move to inside Selection-for H bonded structures Rearrangement- optimise H-bonds, ionic pairs etc. |
| Myoglobin | 8 helices aphipathic binds O2 |
| Ribonuclease | Beta sheets -3strands -3helices degrades RNA H-phobic face of helix against Bsheet |
| Green florescent protein | 11 antiparallel B sheets folds into barrel |
| Bacteriorhodopsin | membrane protien light driven ion pump 7 A helix protein interaction with bilipid layer |
| Domains | seperately folded regions create active sites flexible Same polypeptides |
| Lactoferrin | 4 domains Fe between 2 domains 3 -ve side chains bind to Fe3+ |
| Oliglomeric proteins | more than 1 polypeptide chain separately folded subunits quaternary structure |
| Hemoglobin | 2Alpha Beta regions 4 heme bind 4 Fe and 4O2 Hbonds, Hphobic, salt bridges |
| Hb and Mb | Hb-binds O2 when concentration is high, lungs Mb-binds O2 concentration low, tissue |
| Antibodies | Y-shaped 2 heavy 2light chains neutralize foreign molecules highly specific recognition sites |
| molecular recognition at binding site | -shape -size -charge -non/polar |
Created by:
meglet
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