BIOL 2012 Genetics
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This 3 page Class Notes was uploaded by Chris Bonty on Thursday February 4, 2016. The Class Notes belongs to BIOL 2012 at a university taught by Bethany Zolman in Spring 2016. Since its upload, it has received 13 views.
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Date Created: 02/04/16
Week 4 notes Genetics -know how to draw general structure of amino acid - can be NH3+ and CO2- on acid as well - amino acids come together forming a condensation reaction water out - memorize amino acid codes - Amino acid mutations to consider (size and charge changes) - some times NH3+(N) and CO2-(C) -Primary sequence - secondary structure - Conformation most energetically stable folded protein shape - Beta sheets - tertiary structure - Heme Group: - quartary structure: - Dimers, trimers, and multimers, dimer of dimers? - Homodimers - Heterodimers - Protein Domain: region of protein with a specific function - 3:1 nucleotide:codon - code specific from nucleotide to amino acid - 3 amino acids per 1 protein - MET start codon methianene - Stop codons - Multiple ways to encode for an amino acid - degenerate: all 64 combinations encode for something and its redundant multiple ways to encode - 3-D structure of protein most important - look at a region of a gene and id a transcription initiation site - Open reading frame (ORF) makes the protein - mrna always biger than the protein due to untranslated region - Reading codons of 3 qs 1 amino acid - Always start with ATG (methionine) - be able to identify all these things - need an un translated region to grab onto and start things - Practice met, His, Cys, Ala, Arg, Asp, Ser = M (polar),Y( Polar),C(polar),A(np),R(basic),D(acid),S(polar) - - practice relating codons into amino acid names and characteristics of the acids - May see a DNA strand like in slide 12 on the exam - Transfer RNA mentioned - Has an anti codon sequence (antiparallel) - ending sequence matches protein directly - TENA synthesis: -tRNA synthetase: enzyme that creates follwows a repetitive cycle - 70 S prokaryotic ribosome broken into to parts 50S and 30 S protein complex - Know that all organisms have them and the 50 S includes 2 ribosomal RNAs and 31 proteins -Other has 21 proteins and 2 RNA’s - In depth on Ribosomal complexes - Large sub unit adds in amino acids -Small sub unit reads E site or exit site P site is the reaction site for forming peptide bonds A site is the entry site - new - reactive groups are currently/entering A site - Un charged Trna come out of e site - Have to be a matching tRNA to bind - After entry it allows proximity for amini acids to be added into growing peptide chain - Start codon is there for ribosome to see and be signaled - Ifs are initiation factors - After large substrate we have 3 binding sites - Eukaryote cap at the beginning of untranslated region, here for RNA to grab onto. - non ribosomal elongation factors - GDP is rerleased then next trna comes in - Stop codons, are regions of the mRNA in the A-site - Release factors have compliments too, - Protein folding that affects protein activity - Phophorylation - Proteins have to be transported to the proper place to do their job - Protien has encoded info to get where it needs to go - Different kinds of signals and transports - Ubiquitin and proteasomes involved with protein - Ubiquitin is a tag for degradation by the proteasome - Know the degradation cycle - protein regulators aid selecting tagged proteins - Malfunctioning proteins - 4 kinds of mutation - substitution mutation, 1 nucleotide changing forming the wrong amino acid - A nonsense mutation also a1 base pair change but it forms a stop site - Insertion and deletion mistakes, moves everything in the sequence by one - Silent mutation that doesn’t reflect in change, the third nucleotide change of the third nucleotide not changing the amino acid -
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