Chapter 15 Flashcards
one gene, ___ polypeptide
one
All enzymes are ___, but not all ___ are enzymes
proteins
What is an amino acid structure?
NH2-CHR-COOH
Define polar bonds.
covalent bond that shares electrons unequally
How are amino acids linked?
covalently by peptide bonds
What is are the phases of the protein structure?
Describe them.
primary:
- amino acid sequence
secondary:
- alpha helix or beta-pleated sheet
- peptide linkage and h-bonds
tertiary:
- polypeptide
- h-bonding, ionic bonding, s-s bonding (N-C), hydrophobic effect
quaternary (doesn’t always occur):
- protein
- polypeptide bonding
What are the types of stop codons?
- UAA
- UAG
- UGA
What is the wobble effect?
3rd nucleotide of the codon can vary
- due to degeneracy of the genetic code
What is the name for the AUG codon?
- E. coli:
- Eukaryotes:
- N-formylmethionine
- methionine
What is tRNA charging?
the attachment of a tRNA to its appropriate amino acid
- to the 3’ OH
- ATP is required
Initiation: (translation)
What is the order of bind?
- small ribosomal subunit to tRNA
- initiation factors (proteins)
- larger ribosomal subunit
How is translation/initiation different between E. coli and Eukaryotes?
E. coli:
- mRNA binds to sm subunit
- tRNA has N-formylmethionine
Eukaryote:
- mRNA is not directly involved
- start codons can be anywhere
- there can be more than 1 poly-cistronic mRNA
- tRNA has methionine
- GTP is used
Initiation: (translation)
Methionine is on the beginning of protein. What is this region call?
amino terminus (N-terminus)
Which direction is the protein formed?
n-terminus –> c-terminus
(amino) –> (carboxyl)
Elongation:
the Ribosomal small and large subunits share three sites to bind and interact with tRNA. What are they?
E: exit
P: peptidyl
A: aminoacyl