Lectures

Question 1

Lecture 2- Thermophiles

Answer 1

Stable(thermophiles), denaturing of Structure(proteins)
Protein stability- Avoid Cys and Thr, prefer Arg and Tyr, hydrophobic interiors
Membrane Stability- packed tighter less movement, permeability(proton) effected my motion
Metabolism- use sodium/proton transport
Genetic- low rate of mutation(2009)(favour stability), select for advantageous ones. High no. of proteins for related to folding. High NDN codons(non-polar, hydrophobic residues)
Deep Sea Baccy- lack basic metabolisms- coevovled with others
Uses: TAQ pol (used in PCR), high temp in industry.

Question 2

Lecture 3- Physcophiles

Answer 2

Low temp- biochemical rates, membrane fluidity, protein flexibility decrea
cryoprotectants- Antifreeze glycoprotein(homologus recombination), threhalose(nematodes) protect membrane
Freezing tolerance- secrete solvents/solutes/enzymes, c.nivalis(brightly coloured spores) to melt ice around for use.
Membrane- short acyl chains, high unsaturated fatty acids- up flexibility
Protein Flexibilty- prefer small neutral AA groups than charged, basic, aromatic and hydrophobic groups.
Enzymes-reduced H-bonds and hydrophobic interactions, intersubunit and solvent interaction. clustering glycine residue(low proline and arginine
Cold shock Proteins- nucleic acid secondary structure

Question 3

Bioremediation

Answer 3

Techniques to overcome low nutrient conditions- Biostimulation and bioaugmentation

Question 4

General info

Answer 4

bioprospecting- important in finding out lineages of bacteria(Xenobiotics and phycrophiles)

Question 5

XenoBiotics

Answer 5

Drives evolutionary change

standing genetic variation, single major or polygenic effected, cost of adaptation