Unit 2 Learning Objectives Flashcards
Know the definition of translation
the sequence of bases in mRNA specifies the order in which amino acids are added to a polypeptide chain
Know the factors required for translation
Messenger RNA
Initiation Factors
Elongation Factors
Release Factors
Aminoacyl tRNA synthetases
Transfer RNA
Ribosome (rRNA & ribosomal proteins)
Know the structure of the ribosome and describe the three binding sites for tRNAs
definition: complex structure of RNA and protein that bind mRNA and
control translation
structure:The large subunit of the ribosome contains three binding sites for transfer RNA (tRNA)
subunits:
A (aminoacyl) site
P (peptidyl) site
E (exit) site
Describe the properties of codons and reading frames
codon: group of the 3 adjacent nucleotides in an mRNA that code for an amino acid
reading the sequence of nucleotides
Compare eukaryotic and prokaryotic ribosomes
Know the structure of tRNA and describe key features of the tRNA molecule
-Translation of the message in mRNA is carried out by tRNA molecules: 70-90 nucleotides long, each with its own self-pairing structure
-All tRNAs have CCA at their 3’ end with 3’ –OH group of the A as the attachment site for an amino acid
Know the function of tRNA Synthetase and describe its role in charging tRNAs
Function: connect specific amino acids to specific tRNA molecules
Role in Charging DNAs: A tRNA without an amino acid attached is uncharged; a tRNA with an amino acid attached is charged
Describe the base pairing properties between codons and anti-codons
-The first base in the codon in mRNA (5’) pairs with the last base in the anticodon of the tRNA (3’): antiparallel
-Codons specify amino acids according to the genetic code
-The codon that initiates translation is AUG: corresponds to the amino acid methionine
Describe the degeneracy of the genetic code and know how to read the codon chart
Many amino acids are specified by more than one codon: the genetic code is redundant or degenerate
Compare translation initiation in prokaryotes vs eukaryotes
Prokaryotes: mRNAs lack a 5′ cap; the initiation complex forms at one or more internal sequences in the mRNA: Shine–Dalgarno sequence
Eukaryotes: initiation complex forms at the 5′ cap and scans along the mRNA until it reaches the start codon AUG
Describe the process of translation initiation and the role of initiation factors
Initiation requires Initiation Factors:
i. bind to the 5’ cap of the mRNA
ii. recruit the small subunit of the ribosome
iii. bring up a transfer RNA charged with Methionine
Describe the process of translation elongation
The ribosome moves one codon farther along the mRNA:
- tRNA in the E site is ejected
- tRNA in the P site is moved to the E site
- tRNA in the A site is moved to the P site
- A site is open and available for the next tRNA
Describe the process of translation termination and the role of release factors
-Elongation continues until a stop codon is encountered (UAA, UAG, UGA)
-Release Factor protein binds the A site of the ribosome: causes the bond connecting the polypeptide to the tRNA in the P site to break
-The breaking of the bond creates the carboxyl terminus of the polypeptide
Know the structure of an amino acid
Know how amino acids are classified based on the structure and atomic makeup of their R group
Grouped based on :
i. how they interact with water (hydrophillic or hydrophobic)
ii. whether they are basic or acidic
iii. whether they are polar or nonpolar
Compare hydrophobic and hydrophilic amino acids to one another
HYDROPHOBIC:
Located in the interior of folded proteins in order to be kept away from water
HYDROPHILIC:
-Polar side chains: hydrophilic and tend to form hydrogen bonds with one another or with water molecules
-Basic and acidic amino acids are strongly polar and hydrophilic.
-Basic amino acids: positively charged
-Acidic amino acids: negatively charged
-The charged groups can form ionic bonds with one another and with other charged molecules
Know the three special amino acids and describe the effect these amino acids have on the proteins that incorporate them
Glycine: R group is hydrogen: symmetric
Nonpolar and small: the hydrogen side chain allows for freer rotation around the C-N bond
Glycine increases the flexibility of the polypeptide backbone
Proline: R group is linked back to the amino group:
restricts rotation of the C-N bond
puts constraints on protein folding in proline’s vicinity
Cyestine: contains a –SH (sulfhydryl) group
Two cysteines together can form S-S disulfide bonds: bridges that can connect different parts of the same protein or different proteins
Know the properties of peptide bond formation
-The carboxyl group of one amino acid reacts with the amino group of another amino acid releasing a molecule of water
-The C=O group in the peptide bond is known as a carbonyl group and the N-H group is an amide group
- retrieve the slide lol
Know and compare the four levels of protein structure
1°: Primary structure: sequence of amino acids
2°: Secondary structure: interactions between stretches of nearby amino acids
3°: Tertiary structure: 3D shape of a protein
4°: Quaternary structure: protein subunits interacting with one another
Describe the processes of protein denaturation and renaturation
Know the functional role of chaperone proteins in the folding of polypeptides
Know and compare the cellular components of prokaryotic and eukaryotic cells.
Know and compare protein sorting in the cytosol and protein sorting in the rough ER.
Describe the process of transmembrane protein targeting.