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by: keaffaber.3

Macromolecules BIO 1120-01


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Week 3 notes
Cells and Genes
Professor Dan E. Krane
Class Notes
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This 7 page Class Notes was uploaded by keaffaber.3 on Friday September 16, 2016. The Class Notes belongs to BIO 1120-01 at Wright State University taught by Professor Dan E. Krane in Fall 2016. Since its upload, it has received 18 views. For similar materials see Cells and Genes in Biology at Wright State University.


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Date Created: 09/16/16
Macromolecules Professor Krane 09-08-2016 Carbon’s Bonds  Chemistry involving carbon molecules is often referred to as organic chemistry Valences  Carbon has a valence of 4, which makes it capable of being involved in incredibly versatile molecules  Each of the 4 different functional groups can bind to it and can also form long chains and rings Isomers  Structural isomers have the same chemical formula but functional groups are arranged in different ways  Stereoisomers are molecules that mirror images of each other and all have asymmetric carbon Functional Groups  Seven functional groups that are often associated with carbon are of particular importance to living things o Hydroxyl groups – R-OH, called alcohols, polar like water, assists in water solubility  Immediately think this molecule is a little bit water soluble o Amino groups – R-NH ,2called amines, often acts as a base and hence confers a +1 charge to carbon molecules  Can pick up a H from the surrounding solution Carbonyl groups – R-C=O, called aldehydes, when at the end of a o carbon chain and ketones when in the middle  Carbon with a double bond to oxygen  More water soluble o Carboxyl groups – R-COOH, acetic acid = CH -C3OH, the H is + easily lost due to high electronegativity of both of the O’s in such close proximity  Carbonyl with a hydroxyl group stacked right on top of each other  Organic acids  Very water soluble o Methyl groups - R-CH 3, associated with the hydrocarbons. Methyl groups confer hydrophobic, non-polar patches to carbon molecules  Affects the expression of genes  Arrangements of methyl groups in male and female sex hormones affects their shape and function  Create a hydrophobic pocket that attracts other molecules with hydrophobic pockets o Sulfhydryl groups – R-SH, called thiols, often involved in protein stability, behaves something like a hydroxyl group in the terms of water solubility  Does allow for cross-linking, which helps stabilize protein structures Phosphate groups - R-PO o 4, called organic phosphates, are associated with high energy bonds, and often cause molecules to be acidic (conferring a -1 charge to the carbon molecule)  Potential to react with water  Chemically reactive Polymers  Dehydration reaction (Condensation Reaction): synthesizing a polymer HO-1-2-3-H / HO-1-H o Short polymer + Hydrogen / HO + unkinked polymer  Dehydration removes a water molecule, forming a new bond Removes water molecule H O 2 o Creates a long polymer HO-1-2-3-4-H  Molecules linked together by joining many similar or identical small subunits called polymers  Hydrolysis: Breaking down a polymer HO-1-2-3-4-H o Adds a water molecule breaking the bond – H O 2 HO-1-2-3-H + HO-1-H Carbohydrates  Sugars and their polymers  For every carbon in the molecule there is a water molecule associated with that molecule C-H O 2 Monosaccharides  Typically, multiples of the formula CH 2 such as glucose (C H 6 12 6 and ribose (C H O ) 5 10 5  In aqueous solutions, most sugars form rings or circular structures  Glucose is an aldehyde (Aldose) while a structural isomer, fructose, is a ketone (Ketose). Disaccharides  Two monosaccharides linked together are a disaccharide  The link between them is a glycosidic bond  Two monosaccharides are joined together to form a disaccharide during condensation reactions Polysaccharides  many organisms use very long polymers of sugars as a primary site of energy storage  Long strings of glucose aka starches have 3 different specific names o Amylose o Amylopectin o Glycogen  Cellulose: An alternative, geometric isomer of glucose is also used to make a different polysaccharide that may look similar structurally but has very different properties  Cellulose and chitin are not used for energy storage but rather as structural supports  Cellulose is considered the most biomolecule on earth Lipids  Very diverse group of biomolecules that is mostly made up of stretches of hydrocarbons rich with non-polar bonds that confer upon their molecules a pronounced hydrophobicity Fats  Fatty Acid – long string of carbons (16-18) with a carboxyl group at one end.  Saturated fats – those that have many hydrogens bound to the carbons as possible o Solid at room temperature (fat, lard, butter)  Unsaturated fats – Have one or more double bonds between their carbons o Liquid at room temperature (vegetable oil)  Large amounts of energy are stored in the bonds of fats o Even more is present in polysaccharides (bond for bond)  Most fats organized as triacylglycerides o Triacylglycerides – grouping of 3 fatty acids held together at their carboxyl ends by linkages to a 3-carbon molecule called “glycerol” Phospholipids  structurally related to fats but instead of having a glycerol (C3 8 3) hold three fatty acids together, phospholipids use a phosphate group to hold two fatty acids together  Characteristically hydrophobic at one end and hydrophilic at the other  Primary component of all cell membranes Others  Steroids qualify as lipids o Are hydrophobic o Set of 4 hydrocarbon rings linked together  Waxes are another type of lipid Proteins  The molecules that do the physical work of governing and facilitating the various chemical reactions necessary to life  Play important structural role Amino Acids  Building blocks of proteins  20 different amino acids can combine to form polymers  Chemically reactive groups of amino acids are represented with R o Also known as side chains  R groups of amino acids fall into four groups: o Non-polar o Polar o Negatively charged (glutamic and aspartic acids) o Positively charged (arginine, lysine and histidine) 1°, 2°, 3° and 4° structure  The role that a protein plays depends on the way it is arranged in the R group  The primary structure is known as the proteins unique linear ordering of amino acids o Insulin is a string of 51 amino acids that appear in a different order than the 191 amino acids of human growth hormone  Linear ordering of chemical groups that are coded for in our genes can give rise to predictable sets of bends and turns that make up the protein’s secondary structure  Two fundamental secondary structures: o Alpha helices and beta sheets o Proteins get either depending on the primary sequence of amino acids  At higher levels of structure, all proteins are also folded back upon themselves which gives rise to the tertiary (third) structure o Proteins have a natural tendency to keep their hydrophobic R groups pointed away from water o Hydrophilic R groups are the opposite and point themselves towards water  Quaternary (fourth) structures refer to the level of organization o Proteins begin to interact with outside proteins  Hemoglobin for example is able to carry oxygen in our blood to our tissues in an efficient way only when it is two proteins can combine together in a tetramer – two alpha and two beta globins all together Nucleic Acids  Responsible for giving the instructions to keep everything working together  The ordering of 4 subunits that contain virtually all the information that is needed to keep everything going within all living things on earth  Genes – units that code proteins  DNA (deoxyribonucleic acid) – the genetic material that organisms inherit from their parents  A nucleotide has three parts: o Nitrogenous base  Pyrimidines (cytosine, thymine, and uracil)  Purines (guanine and adenine) o Pentose sugar o Phosphate group  Polynucleotides are linked together by phosphodiester bonds between the phosphate and sugar


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