Bio I Chapter 5 Professor's Notes
Bio I Chapter 5 Professor's Notes BSC 2010
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This 4 page Class Notes was uploaded by Marla Notetaker on Wednesday September 7, 2016. The Class Notes belongs to BSC 2010 at University of South Florida taught by Dr. Eric M. Sikorski in Fall 2016. Since its upload, it has received 49 views. For similar materials see Biology I Cellular Processes in Biology at University of South Florida.
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Date Created: 09/07/16
Chapter 5 Biology I Concept 5.1 Macromolecules are polymers built from monomers Polymers long molecule consisting of many similar identical blocks linked by covalent bonds Monomers I. The Synthesis and Break down of Polymers + - Synthesis: when 2 monomers unite they do so through H and OH therefore water is released. Hydrolysis: breaking down the polymer because water molecules have to break Concept 5.2 II. Sugars a. Classification of the carbohydrates - Aldose: terminal carbon - Ketoses: NOT in terminal Carbon - Pentose: 5 carbons - Hexos: 6 carbons * The 5 (pentose) and Hexoses carbon sugars actually exist in RINGS* *Glycosidic bond: b. Storage: Glycogen: - Liver: to turn back into glucose to release into the bloodstream to maintain the sugar in blood - Skeletal muscle: to contract Starch: in plants Structure - Cellulose - Chitin - Bacterial Cell wall *Alpha glucose is for energy and Beta glucose is for structure* Concept 5.3 Lipids They are groups because they do nor mic well I. Fats - Saturated: if there is no double bonds between carbons in the chain - Monounsaturated: have one double bond of carbon - Polyunsaturated: have more than 1 double bond a. Essential Fatty acids - Omega 3 ad Omega 6: important to make neurons’ cell membrane and improve cardiovascular health b. Major functions of fats: - Energy storage - Insulation - Protection II. Phospholipids – amphipathic (polar and non-polar regions) - Form bilayers: because they want to get away from the other polar molecules they start folding within itself – lowest energy state (where these molecules are happy) III. Steroids: Estradiol – signal - Testosterone - Progesterone - Aldosterone Cholesterol Concept 5.4 Proteins Accounts for more than 50% of the dry mass of most cells Enzyme: catalysis of a reaction Defense: antibodies, complement Transport: channels, pumps, carriers. Structure: cytoskeleton Movement: muscle tissue Signaling molecules: signals cells to do something I. Amino Acids R H N – C – COOH 2 H We have 20 amino acids – 12 essential (the body itself can make them)… 8 essentials (from food) II. Structure Peptide: single or chain of amino acids *DONE BY DEHYDRATION* Proteins: peptides which have a function DNA: determines the sequence of amino acids * Any peptide starts with NH (a2ino) and with a COOH (carboxyl) end a. Shape determines function: proteins should be rightfully folded Primary structure: sequence of amino acids – comes from DNA Secondary structure: hydrogen bonding is responsible – occurs between the amino and carboxyl of the backbones – this is good because all the R groups are pointing AWAY from the coil (helix) so it can interact with other stuf - Alpha – helix - Beta – sheet Tertiary structure: strong covalent bond used to keep the protein from unfolding (disulfide bond) Quaternary structure: multiple structures form and associate to make a functional protein b. What determines Protein Structure? Alterations in: - pH - Salt Concentration Other ways to afect structure: - Adding molecules o Acetyl o Methyl o Phosphorylation Alzheimer Disease is caused by a protein that misfolded however this change is more stable than the original structure, therefore it stays that way c. Protein Folding Chaperonins: helps to changes the proteins (fold them) Ionic Compounds around 250 mM (miliMolar) K with proteins. Concept 5.5 Gene – a unit of inheritance Phosphodiester bond: bonding phosphate to the C-3 of the other nucleotide DNA is negatively charged All the bonds is made between the sugar and the phosphate Proteins are positively charged therefore its very attracted to DNA H-bonds between the nitrogenous bases that are sticking out – antiparallel Adenine can form 2 double bond as well as thymine Guanine can form 3 double bond as well as Cytosine ATP – These can all exist Chargaf’s rule GTP TTP UTP CTP The Hydrogen bond in the double helix is for easier separation RNA is able to fold back in itself and make bonds with itself (transfer RNA) DNA sequence coding for physical traits = gene Creation RNA is the expression of DNA Reading mRNA and synthesize according to that reading (order coding) o Transcription: from DNA to RNA o Translation: take the mRNA through ribosome Central Dogma og Molecular Biology: DNA -> RNA -> Protein Replication: making a copy of DNA