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Protein Structure, Function, and Synthesis
Amino acid
The building blocks of proteins
Peptide bond
A covalent bond between amino acids
Primary structure
A linear sequence of amino acids that form a polypeptide chain and determines the secondary, tertiary, and quaternary structure of proteins
Secondary structure
Describes the conformation of proteins of the polypeptide chain. Results from hydrogen bonding between neighbouring amino acids of the polypeptide backbone and can form an alpha helix or beta sheet
Alpha helix
Forms due to hydrogen bonds to the fourth amino acid neighbour above and below in the spiral and let molecules that are not nearby in the main structure to interact with one another
Beta sheet
Segments of the polypeptide lying side by side in a folding conformation. Sheets can be parallel or antiparallel
Tertiary structure
Described the conformation of the entire protein in a 3D shape and determines the functional form of the protein. This structure is determined by the spatial distribution of hydrophobic and hydrophilic R groups and chemical interactions between the R groups
Quaternary structure
The spatial arrangement of subunits. The polypeptide chains in each subunit can be identical or non-identical
Translation
A sequence of bases in mRNA used to specify the order of amino acids added to the polypeptide chain
mRNA
Primary transcript developed during transcription
Ribosomes
Protein factories where translation occurs. Ribosomes consist of a large subunit and a small subunit
A site
Space in the ribosome where aminoacyl tRNA enters
P site
Space in the ribosome where the growing polypeptide chain is held
E site
Space in the ribosome where empty tRNA exits the ribosome
Codon
Nucleotide combinations that code for the amino acid placement
Anticodon
Complementary sequence of three nucleotides pairs with the codon to deliver the correct amino acid
Reading frame
Dividing a nucleotide sequence of an RNA or DNA molecule into codons that direct protein synthesis
Transfer RNA
A physical adapter between mRNA and the amino acid sequence that pairs anticodons with a complementary codon on the mRNA
Aminoacyl tRNA synthetases
tRNA with an amino acid attached to be added to the growing polypeptide chain
Genetic code
64 codons specify 20 amino acids that are read from 5’ to 3’
Start codon
Initiates translation (AUG)
Stop codon
Terminates translation (UAA, UAG, UGA)
Translation initiation
The small ribosomal subunit and initiation factors scan the mRNA for the start codon
Translation elongation
Aminoacyl tRNA enters the A site and base pairs with the next codon. The ribosome shifts one codon to the right leaving an uncharged tRNA in the E site, peptide bearing tRNA in the P site, and the A site is free for the next charged tRNA
Translation termination
A protein release factor binds to the A site at the stop codon and the polypeptide chain is complete
Initiation factors
Proteins that bind to ribosomes and help assemble the translation initiation complex
Release factors
Proteins that terminate protein synthesis by recognizing stop codons and releasing the polypeptide chain from the ribosome
Shine-Dalgarno sequence
The initiation complex is formed at one or more internal sequences present in the mRNA in prokaryotic translation. There is no 5’ cap or mRNA molecules
Polycistronic mRNA
Primary transcripts contain information for more that one gene in prokaryotes
Gene regulation
Not all genes are expressed in the cell at the same time
Protein translational modifications
Changes made to the protein after translation
Protein sorting
The cell delivers newly synthesized proteins to their correct intercellular or extracellular destination based on specific signal sequences
Protein sorting - No signal
Stay in cytosol
Protein sorting - Amino terminal signal
To chloroplast or mitochondria
Protein sorting - Integral signal
To nucleus
Signal recognition particle (SRP)
Binds to the specific amino terminal signal and transports proteins to the endoplasmic reticulum