IMED1001 Study Guide - Midterm Guide: Motility, Ovalbumin, Enzyme
LEARNING OUTCOMES LECTURES 7-9
Lecture 7:
- Non-covalent bonds in protein structure: determines shaoe of protein (stabilises
structure)
- Primary = sequence of AA
- Secondary = repeated folding of AA (alpha and beta)
- Tertiary = Bonding and folding of alpha and beta
- Quaternary = assembly of subunits
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- Protein domains = able to independently fold to form compact stable structures
- Simple protein = proteins that only contain AA, no other chemical groups
- Conjugated protein = proteins that contain AA and other chemical groups (eg. Lipoproteins,
glycoproteins, metalloproteins
- Prosthetic group = the non-amino acid group in conjugated proteins
Lecture 8:
- Native protein: when it is properly folded and is operative and functional
- Denatured protein: when protei’s coforatio is destroyed, ad caot fuctio orally
- Process of denaturation:
1. Native protein loses biological activity
2. Secondary, tertiary and quaternary structure destroyed
3. Primary structure remains
- Agents that cause denaturation:
1. Heat
2. Chemicals
➔ R.A.: destroys disulphide bonds
➔ Acids, bases, salts: affect salt bridges and H bonds
➔ Detergents: opens hydrophobic regions (in tert struct, hydrophobic cluster in center)
➔ Heavy metals: interacts with sulfhydryl group (-SH)
- Protein function: DOTMESSRN
1. Defense: antibodies
2. Others: anti-freeze proteins
3. Transport: Hb
4. Motility: actin, myosin
5. Enzyme: lipase
6.
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Document Summary
Non-covalent bonds in protein structure: determines shaoe of protein (stabilises structure) Secondary = repeated folding of aa (alpha and beta) Tertiary = bonding and folding of alpha and beta. Protein domains = able to independently fold to form compact stable structures. Simple protein = proteins that only contain aa, no other chemical groups. Conjugated protein = proteins that contain aa and other chemical groups (eg. lipoproteins, glycoproteins, metalloproteins. Prosthetic group = the non-amino acid group in conjugated proteins. Native protein: when it is properly folded and is operative and functional. Denatured protein: when protei(cid:374)"s co(cid:374)for(cid:373)atio(cid:374) is destroyed, a(cid:374)d ca(cid:374)(cid:374)ot fu(cid:374)ctio(cid:374) (cid:374)or(cid:373)ally. Process of denaturation: native protein loses biological activity, secondary, tertiary and quaternary structure destroyed, primary structure remains. Agents that cause denaturation: heat, chemicals. Acids, bases, salts: affect salt bridges and h bonds. Detergents: opens hydrophobic regions (in tert struct, hydrophobic cluster in center) Heavy metals: interacts with sulfhydryl group (-sh)
