Bio 1030 Final Flashcards
Central Dogma
DNA transcribed into RNA, which is translated into protiens
Protiens
Linear polymers of amino acids -> form 3D structures w/ specific functions
Also called polypeptides
Translation
Process in which sequence of bases in mRNA specifies the order of successive amino acids in the protein chain that is forming
How do proteins evolve?
Through mutation and selections and combining functional units
Amino acid structure
composed of amino group bonded with carbon which is bonded to a carboxyl group and a R group
R group determines which amino acid it is
R groups
20 groups total
Allow amino acids to be grouped by characteristics
R group properties
Hydrophilic/hydrophobic
Basic or Acidic
Polar or non-polar
Hydrophobic Amino acids
Avoid water
Internal in proteins
Bonds stabilized with weak van der waals forces
Hydrophilic Amino acids
Polar molecules -> contain electronegative elements
Tend to be located on outside of protein
Basic/acidic amino acids
Basic - positively charged
Acidic - negatively charged
Tend to bond with each other
strongly polar and hydrophilic
Glycine
special amino acid
non-polar and small
increases flexibility of polypeptide backbone
Proline
special amino acid
R group linked back to amino acid
prevents the protein from being as flexible
Cysteine
Special amino acid
contains a SH group
can loop and bind protein structure
Peptide bonds
Covalent bonds between amino acid monomers
carboxyl group of one amino acid reacts with the amino group of another amino acid, releasing water
Primary structures
Primary: Amino acid sequences
Determines secondary and tertiary structures
Secondary structures
Result from hydrogen bonding between amino acid functional groups
two types:
1. Alpha Helix: polypeptide chain twisted tightly in right-handed coil.
2. Beta Sheet: polypeptide chain folds back on itself
Tertiary Structures
Result from spatial distribution of hydrophilic and hydrophobic R groups as well as other interactions between the R groups
Gives protein 3D shape
Determines protein function
Ribosomes
Where translation takes place
Consist of a small subunit and large subunit
Determines correct reading frame of codons
Codon
A group of three adjacent nucleotides coding for a single amino acid
Ribosome Large Subunit
includes 3 binding sites for molecules of tRNA
A (aminoacyl)
P (peptidyl)
E (exit)
tRNA
conduct translation
contain 70-90 nucleotides
bonds back with itself
3 bases in loop make up the anticodon
tRNA synthetases
Connect specific amino acids to specific tRNA molecules
uncharged with no amino acid attached
Anti-codon
interaction with codon determines base pairing
First base in the codon in mRNA pairs with the last base in the anticodon (must be antiparallel)
Codon that starts translation is AUG
Translation Process
- Initiation
- Elongation
- Termination
Initiation factors
bind to the 5’ cap of the mRNA
bring up tRNA charged with methionine
Next tRNA joins ribosome and scans the mRNA until the first AUG is encountered
Elongation
1.Once the new tRNA is in place, a coupled reaction takes place in which the bond connecting the Met to its tRNA is transferred to the amino group of the next amino acid in line as the first peptide bond is formed.
2.The new peptide is now attached to the tRNA in the A site.
3.Formation of the peptide bond requires multiple proteins in the large subunit, but the RNA in the large subunit is the actual catalyst.
4.The ribosome then shifts one codon to the right, which moves the uncharged tRNA (Met) to the E site and the peptide bearing tRNA to the P site, freeing the A site for the next charged tRNA in line.
5.The tRNA in the E site is ejected.
6.A covalent bond forms between the amino acid bonded to the tRNA in the A site and the next amino acid.
7.The subunit moves down one codon.
Termination
1.The process continues until one of the stop codons is encountered (UAA, UAG, UGA).
2.When the stop codon is encountered, a protein release factor binds to the A site of the ribosome, causing the bond connected to the polypeptide of the tRNA to break.
3.The breaking of the bond creates the carboxyl terminus of the polypeptide and completes the chain.
Selection of Proteins
1.These mutations can be retained or eliminated through selection based on the ability of individuals with the mutation to survive and reproduce.
2.If the mutation improves protein function, the individual will reproduce more successfully than others, and the mutation will eventually spread throughout a population over time.
Mutation
Any heritable change in genetic material
Heritable
Mutation is stable and therefore passed on through cell division
RNA mistakes
Not-heritable and common
Single nucleotide polymorphism
single change in the genome
linked SNP: occur outside of the gene and to not affect protein function
Non-coding SNP: Occur in regulatory region of gene. Doesn’t change amino acid sequence
Coding SNP: occur in coding region and alter the protein’s function (change amino acid sequence)
Silent Coding SNP: occur in coding region but do not alter protein’s amino acid sequence