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Movement Growth Reproduction Complex Orginization Metabolism Adaptation Use of Energy Responsiveness Variation via Heredity
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99% of all living matter on earth is made up of these elements.
- Carbon
- Hydrogen
- Nitrogen
- Oxygen
- Phospohrus
- Sulfur
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Same Formula different "build" |
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- Comprised of one or a few polypeptides
- Made from a combination of 20 Amino Acids
- These are held together by peptide bonds
- 4 Structure layers
- primary, secondary, tertiary, quaternary
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The addition of genetic material to bacteria - 1928 Griffith & coworkers
- R strain & S strain bacteria in mice
- 1944 Avery & coworkers
- saw similarity between transforming material and DNA
- Hershey & chase (blender)
- Used radioactive sulfur to tag proteins and radioactive phosphorus to tag DNA then blended to see separation. Showed strong findings that DNA was the Genetic material.
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- Watson & Crick brought together the full picture of DNA structure from analysis of the work of others in the field.
- They proposed it was anti parallel
- Double Helix from R. Franklin's work
- Complementary Base pairs (see Chargaff)
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- Watson & Crick
- Semi conservative replication
- Meselson & Stahl
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- Bindin
- Initiation
- Elongation
- Termination
- Processing
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A dictionary that translates between the sequence of Nucleotides in mRNA molecules & the sequence of amino acids in a polypeptide(protein)
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Protein Synthesis - Formation of chains of amino acids linked by peptide bonds
- These bonds are catalyzed by a ribozyme
Three Stages - Initiation
- Elongation
- Termination
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Peptide chain begins to be made at the amino-terminal end. A free amino group at the beginning end A free carboxyl group at the other end
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- Hydroxyl
- Carboxyl
- Amino
- Sulfhydryl
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Fatty Acids Cmany H2many Other few
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Aminoacyl-tRNA Synthetase |
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Catalytically active RNA molecules, work like enzymes |
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A "word in the genetic code. Each is three letters long made from the nitrogenous bases of DNA or RNA (whichever it is being used for). AUGC for RNA ATGC for DNA 4x4x4=64 At least one must be a stop codon, in mRNA there are 3 stop codons |
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Primary Protein Structure |
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The amino acid sequence of a protein is its primary structure. These are held together by peptide bonds
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Secondary Protein Structure |
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The local folding of the chain of amino acids Hydrogen bonds are crucial for secondary structure. Includes the... - Alpha-Helix
- Beta-pleated sheet
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Tertiiary Protein Structure |
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The more global folding of the polypeptide chain. Four forces hold the tertiary structure together - hydrogen bonds
- nonpolar, hydrophobic groups that often come together
- ionic interactions among charged side groups
- bonding of pairs of cysteine residues which contain sulhydryl groups AKA DISULFIDE BRIDGES
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Quaternary Protein Structure |
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If more than one polypeptide make up the protein then it has quaternary structure which holds the chains together. |
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X-ray diffraction, patterns indicated that DNA was helix with certain repeat spacings. Used by Watson & Crick |
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Determined structure of DNA in 1953. Based this on research of Chargaff and Rosalind Franklin. |
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Blender experiment. Identified DNA as the genetic material. Radioactive sulfur (bound to proteins) and radioactive phosphorus (bound to DNA) |
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Semi Conservative DNA replication |
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Each new DNA molecule contains one old and one new strand. |
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Used isotopes to follow the process of the copying of DNA in bacteria. Went from heavy to light isotopes in the nutrients teh bacteria had been growing on. compared the density of the DNA one and two genreations after the shift in isotopes in the bacteria by applying DNA to a density gradient centrifuge. After one generation all of the DNA was of intermediate density (one old one new strand) as predicted. |
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Conservative DNA replication |
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Incorrect theory Would create one entirely new strand and one old molecule (densities would have been different one light one heavy for Meselson and Stahl) |
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A class of protein which unwinds the double helix ahead of the main DNA polymerase molecule. |
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Catalyzes the addition of nucleotides to the new, growing strand, using one of the existing strands as template. Can only copy in one direction along the DNA strand making a new strand that starts from the 5' end and builds towards the 3' end. |
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short segments of DNA on the lagging strand. |
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Links together Okazaki fragments. |
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RNA Primer at the start of each DNA strand is made first. Allows the DNA polymerase to get started. Each Okazaki fragment has this and another pprotein must strip out this primer and fill it in with DNA nucleotides before the ligase links everything together. |
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The words in the language of DNA each one is three letters (nucleotides) long. There are four nucleotides that can make these codons up. |
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The process of making an RNA molecule on a template of DNA. |
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the enzyme that transcribes RNA from a DNA template. Eukaryotes have multiple kinds of RNA polymerase. THe RNA polymerase links nucleotides together to make an RNA molecule and uses the sequence of nucleotides on one strand of the DNA to specify a complementary sequence on the RNA. RNA uses a U nucleotide uracil instead of thymine (T) |
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Binding Initiation Elongation Termination Processing |
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RNA polymerase binds to the DNA at particular sequences along the DNA THe binding regions are called promoters. Special transcription factors, generally proteins, can control the binding of RNA polymerase and the initiation of RNA synthesis. Some of these transcription factors bind directly to the DNA and can promote or inhibit the binding of RNA polymerase or the inititation of RNA synthesis. Other such factors bind directly to the RNA polymerase. |
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The DNA double helix unwinds in a small region, and initiation of synthesis of RNA begins at a specialized initiation site near the promoter region. |
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The RNA polymerase moves along one DNA strand making a compliementary RNA strand which separates from the DNA as the DNA double helix rewinds when RNA polymerase moves along. The RNA chain grows from the 5' to the 3' end. |
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A particular signal sequence along the DNA indicates that the end of the RNA molecule has been reached. RNA polymerase ceases synthesis and separates from the DNA, as does the completed RNA molecule. |
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After synthesis there is further modification to some RNA molecules. |
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Ribosomal RNA participate in protein synthesis. |
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Transfer RNA these are relatively short (75-85 nucleotides long). RNA molecules have single amino acids linked to them, and play a role in then linking the amino acids to the growing polypeptide chain during protein synthesis on the ribosome. |
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Messenger RNA each carries information specifying the sequence of amino acids for a polypeptide. This is the molecule that carries the genetic information from DNA to protein. It is the RNA in the famous information flow formula from molecular biology: DNA-> RNA-> Protein. |
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contain two subunits, large and small. Each contains one or more rRNA molecules plus a variety of proteins. Prokaryotes ribosomes contain a total of three different rRNA molecules and 55 proteins. Eukaryotes have 4 rRNA molecules and about 70 proteins. Ribosomes are created in the nucleolus which contains the DNA that has the genetic info for making rRNA molecules. The proteins that become part of the ribosome are made in the cytosol outside of the nucleus and then transported inside. Small and large ribosomal subunits are shipped from the nucleus to the cytoplasm where they are used for protein synthesis |
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The proteins that become part of the ribosome are made in the cytosol outside of the nucleus and then transported inside. Small and large ribosomal subunits are shipped from the nucleus to the cytoplasm where they are used for protein synthesis |
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- Enzymes which link one of the 20 possible amino acids to particular tRNA molecules.
- The enzymes hydrolyze ATP as they make the linkage.
- tRNA to amino acid bond is an enrgetic bond. it provides energy to form the peptide bond between amino acids in the protein
- AMinoacyl-tRNA synthetases are a key to the accuracy of protein synthesis.
- There is no correction system if the wrong amino acid is placed on the tRNA but it is very accurate.
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Protein synthesis Involves the formation of chains of amino acids, linked by peptide bonds. The formation of peptide bond linkages between amino acids is catalyzed by a ribozyme. Initiation Elongation Termination |
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- The peptide chain begins to be made at the amino-terminal end. There is a free amino group at the beginning end and there will be a free carboxyl group at the other end of the polypeptie.
- There is an initiator tRNA-methionine which recognizes the AUG start codon.
- In prokaryotes, a modified, formylmethionine is the amino acid linked to the initiator tRNA.
- In all organisms, a small ribosomal subunit joins together with an mRNA and the initiator tRNA, and then a large ribosomal subunit joins to complete the initiation complex.
- Other proteins that help in the process are initiation factors, there are also elongation factors and a termination factor.
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- The addition of an amino acid to the growing polypeptide chain. Three substeps
- Binding
- Peptide Formation
- Translocation
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- The binding of the next tRNA is directed by the next codon on the mRNA at a site on the ribosome called the A site (amino-acyl site)
- A GTP molecule is hydrolyzed as binding occurs, and the energy released is (probably) used in the recogniztion process, ensuring accuracy in the linkage between codon and anti codon.
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Elongation Peptide Bond Formation |
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- The amino acid on the new tRNA is bonded to the amino acid chain attached to a tRNA molecule at the P site (peptidyl site).
- This step of peptide bond formation is catalyzed by a piece of rRNA.
- The fact that a ribozyme catalyzes peptide bond formation probably is of significance for the origin and evolution of life.
- The bond formation actually causes the growing polypeptide chain to be transferred to the new tRNA at the A site.
- The old tRNA, on the P site, now without any attached amino acids, leaves the ribosome.
- This leaves the P site temporarily vacant.
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- The tRNA with growing polypeptide attachedm shifts along the ribosome from the A site to the P site, and the mRNA shifts with it, moving one codon over and presenting the next codon on the mRNA at the now vacant A site.
- The vacant tRNA moves from the P site to a newly recognized E site (exit site) on the ribosome.
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Occurs when a stop codon (UAA, UAG, UGA) reaches the A site and a releasing factor binds at the A site and triggers teh breaking apart of the complex. |
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