Textbook Notes (290,000)
US (110,000)
UM (1,000)
BIL (100)
BIL 250 (10)
Chapter 6

BIL 250 Chapter Notes - Chapter 6: Hydrolysis, Kozak Consensus Sequence, Transferase


Department
Biology
Course Code
BIL 250
Professor
Kevin Mc Cracken
Chapter
6

This preview shows page 1. to view the full 4 pages of the document.
CHAPTER 6: Translation
Translation: THe conversion of mRNA to an amino acid and polypeptide sequence
About a protein:
Contains nitrogen
Organic compound
High molecular weight
One or more polypeptides
These peptides are composed of amino acids
Components of an amino acid:
1. Amino Group (NH3+)
2. Carboxyl Group (-COO-)
3. Hydrogen Atom
4. R group (variable for each AA)
About Amino acids:
20 of em
Acidic (Aspartic acid and Glutamic acid)
Basic (Lysine, Arginine, Histidine)
Polar (hydrophilic) (6 of them)
o(Tyrosine, Serine, Threonine) targets for phosphorylation OH group
Non-polar (hates water) (9 of them)
oPrevalent in cell membranes
Protein Phosphorylation:
A post-translational modification where amino acid is phosphorylated by protein kinase
(A phosphate group is added)
Formation of a peptide bond:
When a peptide bond is formed between polypeptides, water is lost :(
This is known as a dehydration synthesis reaction
N Terminus→ polypeptide chain→ C terminus
Four Hierarchical levels of protein organization:
1. Primary- amino acid sequence
2. Secondary- folds and twists into a chain
1. H bonds
2. Tertiary- 3D shape of a single polypeptide
1. Diff R groups
2. Quaternary- many polypeptides in subunits
The genetic code is degenerate: more than one codon can make the same AA
MY MANZ Francis Crick studied Frameshift mutations in bacteriophage T4. This was caused by
Proflavin he could cause and insertion or deletion of base pairs to mutate. When this happened,
different amino acids were produced! Also, r+ mutants that had Proflavin could be restored to
the regular wild type. This because of revertants. Three insertions restored the function.
find more resources at oneclass.com
find more resources at oneclass.com
You're Reading a Preview

Unlock to view full version