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Bio 190 Notes Unit 2 Week1

by: Amy Rice

Bio 190 Notes Unit 2 Week1 Biol 190, Intr biology health profession

Amy Rice
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About this Document

Covers: Gene Expression through RNA Translation Protein Structure
Joanna M. Paterson
Class Notes
Biology, RNA, translation, Proteins




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Popular in Biology

This 4 page Class Notes was uploaded by Amy Rice on Sunday February 21, 2016. The Class Notes belongs to Biol 190, Intr biology health profession at Towson University taught by Joanna M. Paterson in Spring 2016. Since its upload, it has received 30 views. For similar materials see Biology in Biology at Towson University.

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Date Created: 02/21/16
BIOL 190 2/16/16 Small section of HBB (hemoglobin B) is transcribed from a single strand copy of DNA into mRNA. mRNA is then processed into mature mRNA, a shorter strand with a cap and tail. Finally sent through a nuclear pore out of the nucleus, into the cytoplasm to carry out translation. Structure: mRNA- Long coding sequence with cap and tail tRNA- Single strand molecule of 80 bases with amino acid attachment site on one end and anticodon on opposite end rRNA- 2-3 rRNAs and about 50 proteins make up the large subunit of a ribosome and 1 rRNA and ~30 proteins construct the small subunit of a ribosome Role in Translation: mRNA- 1 important ingredient required for translation; carries genetic code for protein tRNA- 1) Pick up appropriate amino acids 2) Recognize appropriate codons in the mRNA rRNA- Creates the binding site for mRNA and tRNA and connects amino acids to the growing polypeptide chain. messengerRNA:  Transcripted from DNA in order to carry genetic coding to be translated in the cytoplasm  The cap (single G nucleotide) and tail (chain of 50-250 nucleotides) facilitate the export of the mRNA from the nucleus, and protects the mRNA from being attacked by cellular enzymes (like the mRNAs own personally secret service body guards, escorting the mRNA to its destination in the cytoplasm), as well as helping bind ribosomes to the mRNA  Introns- internal non-coding regions  Exons- the part of the gene that is expressed (coding region)  Before leaving the nucleus, introns are removed and exons are added to produce a continuing coding sequence  RNA Splicing- the cutting and pasting processes of introns and exons Codons: coding units; sequence of 3 DNA/RNA nucleotides that correspond with specific amino acids Anticodon: The special triplet of bases at one end of the folded molecule AUG is the start of the genetic message; start codon UAA, UAG, UGA are all stop codons The Triplet Code:  3:1 code- 3 nucleotides code for 1 amino acid  Protein language has 20 letters/amino acids transferRNA:  Single-stranded molecule of 80 bases  Amino acid attachment site- where amino acids attach, passed from another tRNA attachment site  3 base sequence that is hydrogen-bonds to codon in mRNA BY complementary base pairing rules  Made in nucleus but functions in cytoplasm  Each tRNA has its own specific loading enzyme  Anticodon- special triplet of bases at one end of the folding molecule (humans not have anticodons) ribosomalRNA:  Made by DNA transcription from particular rRNA coding genes in nucleolus  Large subunit- catalyzes formation of covalent bond between amino acid in protein synthesis (contains peptidyl transferase, an RNA enzyme)  Small subunit- place where mRNA hydrongenly-bonds with tRNA  Small and large pass through nuclear pore separately Ribosome- cytoplasmic structure or organelle; cellular component that is directed by the nucleus in order to carry out protein synthesis Free and bound ribosomes are structurally identical. They can alternate between being suspended in the cytoplasm (free) or attaching to the outside of the nuclear envelope/endoplasmic reticulum (bound) TRANSLATION – When codons and anticodons bind together to create somewhere for tRNA to latch onto in order for amino acids to add onto and grow the polypeptide chain. The tRNA ‘reads’ the coding on mRNA to then be translated into amino acids, while rRNA catalyzes the process. Initiation:  tRNA binds to small subunit  mRNA binds to tRNA and small subunit  small subunit and tRNA travel along mRNA, searching for AUG to start coding  large subunit joins complex Elongation:  tRNA diffuses w/ amino acids to dock at next codon  Correct tRNA comes in because of complementary anticodon  Amino acid breaks off tRNA then covalently links to next amino acid  Old tRNA diffuses away  Translocation- Ribosome moves along mRNA, looking for next codon  Repeat Elongation cycle: o Codon recognition o Bond formation o Translocation Termination:  tRNA comes in contact with stop codon  no further tRNA binds  release factor binds to stop codon  complex disassembles: o finished protein is released into the cell o empty tRNA falls out of complex o ribosomal subunit (small and large) break apart 2/18/16 Protein- biomolecule composed of amino acids; structure enables to carry out function Structures:  Globular- irregular spherical shape; contains many bumps and grooves (many) [helixcase, ligase]  Fibrous- long and narrow; cable like (few) Function:  Transport- moving material into or out of cells [potassium channels, hemoglobin]  Hormones- chemical signaling [insulin, glucagon]  Contractile- contraction [actin, myosin]  Structural- support, toughness [collagen, keratin]  Protection- defend against harm [antibodies]  Enzyme- carry out every reaction within the cell or body (-ase)  Storage- nutrient storage for growing embryo [endosperm proteins, albumin] There are 4 different nucleotides in RNA and 20 amino acids in protein  Bonded to amino group  Carboxyl group  R-group R-group aka side chain differs between each different amino acid R Group:  Size  Charge (+ or -)  Polarity (hydrophilic) o “partial” charge o Unequal sharing of electrons (polar covalent bond) Bending of amino acid chain; small R group allows the bending of the chain; large R groups are more stiff and do not allow for bending Dehydration Synthesis:  Removal of –OH from one amino acid and –H from a different amino acid, in order to release H2O  Allows direct covalent bond between the two amino acids  Water is taken out in order for the amino acids to combine and create one big molecule Polypeptide to protein structure:  Chain of amino acids, produced by dehydration synthesis or translation Primary structure- specific chain of amino acids A linear chain of amino acids cannot function; not a protein, only a polypeptide chain Secondary- coils (helices) and folds (pleated sheets) w’ connecting segments o Due to Hydrogen bonding along the backbone o H-bonds between parts of polypeptide backbone Tertiary- structure folds into 3D shape; generally globular; bonds between R groups  Hydrophobic amino acids huddle together on the inside (non-polar)  Hydrophilic position on outside (polar and charged)  Large loops are hydrophobic  Bonds between R groups stabilize the tertiary structure  Covalent, ionic, and hydrogen bonds hold the tertiary structure together between the R groups Quaternary- functional protein consisting of 2+ individual polypeptide chain  Not all proteins have a quaternary structure  Covalent, ionic, and hydrogen bonds hold the quaternary structure together


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