Class notes 9/1-9/3
Class notes 9/1-9/3 BIOL 3301 - 002
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BIOL 3301 - 002
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This 5 page Class Notes was uploaded by Ashley Lutz on Monday September 7, 2015. The Class Notes belongs to BIOL 3301 - 002 at University of Texas at Arlington taught by Laura D Mydlarz in Summer 2015. Since its upload, it has received 175 views. For similar materials see CELL PHYSIOLOGY in Biology at University of Texas at Arlington.
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Date Created: 09/07/15
quotThe Molecules of Lifequot 0 Living things all share the same categories of molecules 0 Mechanisms at the cellular level are similar among all living creatures Macromolecules 0 Proteins 0 Carbohydrates 0 Fats 0 Nucleic acids Basically we break down the macromolecules into their constituent elements and rebuild what we want out of those Simple sugars monosaccharides bind to each other to form carbohydrates Protiens made from amino acids most important property is ability to fold Lipids unsaturated are healthier saturated are less healthy Lipids are used to form things like cholesterol fatty acids etc Saturated fats are essentially straight which allows them to pack closer together which makes them solid at room temp So solid is unhealthy Unsaturated fats have lots of bends which keeps them from packing closely together So liquid is healthy Nucleotides found in all foods Breaking the Macromolecules 0 Use proteins enzymes Covalent bonds are the strongest bonds at approximately 380 K per mole Requires energy and enzymes to break Hydrogen bonds are much weaker at approximately 4 K per mole Break by changing polarity movement etc Used to hold pretty much everything in the cell together Hydrogen bonds allow for change in shape without destroying the function Proteins used for enzymes lipid bilayer has to shift to allow things in and out of the cell Ionic bonds are in between at approximately 13K per mole Knowing the bonds allows for prediction of what the structure will be used for Most functions of the cell require proteins quotProtein structure determines its functionquot Protein structure levels primary secondary tertiary quaternary supramolecular Primary strand Formed by peptide bonds Secondary alpha helix beta sheets Formed by hydrogen bonding Tertiary real shape More hydrogen bonds sometimes includes disulfide bonds Quaternary multiple proteins folded together Multimeric protein is another term for quaternary structure Structure is determined by the amino acid sequence the side chains on each amino acid interact with the other side chains and these interactions create the tension that holds the protein in it39s shape Classes of amino acids Uncharged Polar uncharged Charged Uncharged amino acids Hydrophobic Form pockets in the protein that do not have water within This is not an interaction between the hydrophobic parts it is a result of the interactions between the hydrophobic structures and the water around them They will be more common in membrane proteins Cysteins are used to form covalent disulfide bonds in the protein Polar uncharged Hydrophilic These will hydrogen bond with water Interact in any water based media cytosol blood etc These form the binding pockets for enzymes to draw in the molecules they will catalyze Posttranslational modification These processes include methylation hydroxylation glycosylation phosphorylation sulfur disulfide bond formation etc Peptide bonds the bonds between amino acids in a polypeptide chain Single covalent bond between two amino acids Connects the carboxyl group of one amino acid to the amine group of the next amino acid 2030 amino acids form a peptide These are relatively small minimal folding and include things such as venoms antibiotics poison etc Less than 300 amino acids is a polypeptide The number of peptides in the chain is less relevant than the fact that they generally do not have a 3D shape They are linear Proteins have 3D shape and are longer than polypeptides If a protein is folded incorrectly or unfolded it will not function Native state the term for the correctly folded protein The folding is the road between the DNA nucleotide sequence and the final function of the proteins Folding usually takes less than a minute to fold Denatured protein has lost its hydrogen bonds and disulfide bonds because of heat change in pH etc Different factors used to denature a protein have different results on the form of the denatured protein Alzheimer39s cystic fibrosis are cause by incorrect folding of the protein When proteins are folded incorrectly they can end up sticking together and blocking the normal function of the cell Proteins are correctly folded when they are in their lowest energy state Proteins generally have a hydrophobic core with little to no space in the middle of the protein The other side chains are sent to interact with the aqueous environment surrounding the protein The only aspect of folding they control is to move toward anything polar causing ionic bonding Disulfide bonds create stability in the folded protein Helices are formed by a hydrogen bond between amine of one and carboxyl of amino acid 4 carbons down Betasheets are formed by hydrogen bonding between different sections of the peptide chain This causes the side chains to be facing alternate directions from one sheet to the next One tertiary structure Helixhelix motif Two secondary structures alpha helices lined up next to each other They are wound together Helixloophelix motif one spiral loops around a calcium ion and causes a straight helix to bend Quaternary structures are held together by hydrophobic effects hydrogen bonds electrostatic interactions and two surfaces between the proteins fitting together perfectly Half of the chemicals in our bodies are proteins Having a limited variety of the building blocks for macromolecules makes it easier to make sure everything is formed correctly and to guarantee that we can find those pieces in our food when we cannot make them ourselves Binding between an enzyme and the substrate causes the entire enzyme to change shape conformation even though there are only one or two amino acid side chains that bind to the substrate Cell Membrane is the gatekeeper determines what goes in and what comes out of the cell Phospholipids are equally hydrophobic and hydrophilic This causes con icting forces pulling the molecule in different directions Result is Mycels and lipid bilayers depending on the amount of phospholipids present Hydrogen bonding stabilizes the structure The hydrophobic interactions are what cause the bilayer to form not the hydrogen bonding Cholesterol for rigidity Proteins are most important part of lipid bilayer Alpha helices form pore for things to travel into and out of the cell
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