Week 4: Gene Expression. Part 3

University:
The Pennsylvania State University
Course:
BIOL 230W | Cellular Biology
Academic year:

2023
Views:

463

Pages:

2
Author:

Sarah Landeck

BIOL 230W - Week 4 Gene expression pt 3 — Ribosome recognizes 5’ cap on mRNA, reads information and translate into polymer of amino acids —> mRNA is translated in the 5’ to 3’ direction! —> once the protein is complete, it needs to fold in order to function —> proteins made from nuclear DNA that need to enter the mitochondria are assisted across the membrane into the mitochondria by transport proteins — Translated proteins are sent through endomembrane system via Golgi —>proteins are translated into ER via a translocon on ER surface — *protein diagram showing functional groups — The larger an amino acid side-chain is, the more hydrophobic it will be — Translation molecules = tRNAs (bring amino acids to ribosome), G-proteins (promote processes), and ribosomes —> the anticodon is complimentary to codon in the mRNA —> aminoacyl-tRNA synthase binds amino acid to tRNA Gene expression pt 4 —> G-proteins need to bind to GTP in order to function (active) — Some RNA in ribosome has ribozyme activity (catalyzes reactions) —> large subunit has A,P,E binding sites, small subunit binds mRNA — 3 stages of translation = initiation, elongation, and —> During initiation, the translation complex relocates to start codon — Wobble pairing on third base pair of a codon allows multiple codons to code for the same protein — At the A site of the large subunit on the ribosome, there is a release factor that allows the ribosome to let go of the nished amino acid chain Gene expression pt 5 — Primary structure is amino acid sequence. Secondary is hydrogen bonds of backbone. Tertiary structure is interactions between are groups. Quaternary is interactions between proteins. —> super secondary structure is more than one secondary structure interacting — Both protein domains and structural motifs represent the functional part of a protein, fi but only protein domains can function outside of the protein