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BSC 114, Week 2-3 Notes

by: Hannah Tomlinson

BSC 114, Week 2-3 Notes BSC 114

Hannah Tomlinson

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About this Document

These are all of chapter 5 notes taken from 8/29-9/7. Macromolecules.
Principles Of Biology I
Kimberly Caldwell
Class Notes
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This 7 page Class Notes was uploaded by Hannah Tomlinson on Sunday September 11, 2016. The Class Notes belongs to BSC 114 at University of Alabama - Tuscaloosa taught by Kimberly Caldwell in Fall 2016. Since its upload, it has received 12 views. For similar materials see Principles Of Biology I in Biology at University of Alabama - Tuscaloosa.


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Date Created: 09/11/16
8/29-9/7 Chapter 5 Macromolecules  Molecules are made by living cells  They are made of carbon and the functional groups  Cells join small organic molecules to form bigger molecules known as macromolecules  4 classes for the molecules -Carbohydrates -Proteins -Lipids -Nucleic Acids  Cells link subunits called monomers into polymers Condensation Reaction  Bond between 2 monomers  Also known as dehydration reaction  The 2 molecules are covalently bonded to each other by losing a water molecule  One has a hydroxyl group and the other is a hydrogen  When the reaction is repeated by adding monomers one by one, it makes a polymer Hydrolysis  Process where polymers are disassembled to monomers  Reverse of the dehydration reaction  Hydrolysis: “break with water” Carbohydrates  Sugars  End in –ose for sugars -e.g.: glucose, fructose  3 types -Monosaccharides (single sugars) -Disaccharides (double sugars) -Polysaccharides (polymers of many sugars) Monosaccharides -3-7 carbons -molecular formula is some multiple of CH O2  Ex. Glucose is C 6 O10 6 -OH group is attached to carbon except one, which is double bonded to an oxygen to form a carbonyl group -major nutrients for cells -in cellular respiration, cells extract the energy stored in glucose molecules -serves as the raw material for the synthesis of other types of small organic molecules, including amino acids and fatty acids -sugars not immediately used are incorporated as monomers into disaccharides and polysaccharides Disaccharides -double sugars -consists of 2 monosaccharides joined by a glycosidic linkage (a covalent bond formed between 2 monosaccharides) -most common disaccharide is sucrose Polysaccharides -polymers of many monosaccharides -consists of a few hundred to a few thousands monosaccharides linked together -2 types  Storage polysaccharides  Structural polysaccharides -Storage polysaccharides  Storage material, digested as needed to provide sugar for cells  Plants store this as a starch  Animals store polysaccharides as glycogen in the liver and muscle -Structural polysaccharides  Serves as a building material for structures protecting cells or whole organisms  In plants, cellulose is a major component of the tough walls that enclose plant cells (fiber)  In insects, chitin is used to build exoskeletons -Difference between starch and cellulose  Different type of covalent bond between the glucose units of the 2 molecules makes one digestible (starch) and the other one is digestible in humans (cellulose)  Chitin can be used as a surgical thread because we cannot digest it Lipids  Hydrophobic  Mostly composed of hydrocarbon, but have some polar bonds associated with oxygen  3 families of lipids -Fats -Phospholipids -Steroids Fats -large molecules constructed from 2 kinds of smaller molecules  Glycerol and fatty acids  From dehydration reaction  Glycerol is an alcohol  Fatty acids are hydrocarbons of 16-18 carbons -nonpolar C-H bonds in the tails of fatty acids are the reason fats are hydrophobic -fats separate from water because the water molecule bonds to another and exclude fats (like oil and vinegar, 3 fatty acids join to 1 glycerol) -Saturated fat  NO double bonds between carbon in the tail  Vary in length and in number and location of double bonds but saturated fatty acids don’t have double bonds -Unsaturated fat  Have one or more double bonds in the tail  Saturated and unsaturated fats differ in hydrocarbon tails -Trans fats  What are they? o Partially hydrogenated fats o Less vulnerable to becoming rancid than original oils (going bad) Phospholipids -main component of our cell membrane -structurally related to fats -only has 2 fatty acid chains instead of 3 and has a phosphate group (on 3 glycerol) -PO 4roup is negatively charged -sometimes other small molecules that are charged or polar can be linked to a phosphate group to form a variety of phospholipids -Phospholipids in cells  At the surface of a cell the phospholipids are arranged in double layer (bilayer)  Hydrophilic head: on outside of bilayer  Tails pointed toward interior of membrane, away from water Steroids -carbon skeletons consisting of 4 interconnected rings -side effects  Acne/oily skin  Enlarged clitoris/penis  Deepened voice  Unusual hair loss/growth  Psychological disturbances  In sexually mature males: enlarged breasts Proteins -account for more than 50% of the dry weight of cells -a human has tens of thousands of different proteins -structurally complex but comprised of amino acids (monomers of proteins) -each type is unique because of the ordering of the 20 amino acids -in humans, the average protein length is 476 amino acids -consists of  Alpha carbon bonded to a hydrogen  Carboxyl group  Amino group  Side chain symbolized by R Amino Acids -processing both carboxyl and amino groups -20 kinds of amino acids- same base formula with distinct side chain (R) Identification of amino acid types 1. Nonpolar R groups will share electrons equally (typically composed of hydrocarbon) 2. Polar R groups- electrons won’t be shared equally (possess functional group like OH and SH) 3. Acidic- these R groups contain carboxyl groups (COOH) 4. Basic- these R groups contain amino groups and have N+ -does not have oxygen associated in the R group  Amino acids come together to form proteins  2 amino acids combined=dipeptide  a polypeptide would be formed when four or more amino acids combine Amino acids are linked to form protein polymers  Condensation synthesis  The carboxyl group of amino acid is joined to the amino group of another  Makes peptide bond  When the process is repeated it makes a polypeptide Polypeptides  N-C-C-N-C-C is the polypeptide backbone  One end of the polypeptide has a free amino group (N)  The other end has a free carboxyl group (C)  The polypeptide chain has polarity with an amino end (called N- terminus) and a carboxyl end (C-terminus) Protein confirmation  Proteins form 3-D shapes that are important for how proteins function  4 levels -Primary -Secondary -Tertiary -Quaternary Primary  Unique sequence of amino acids of a protein -e.g.: transthyretin is 127 amino acids long  This protein transports vitamin A in our blood Secondary  The folding of a polypeptide chain due to hydrogen bonds at regular intervals along the polypeptide backbone or skeleton.  2 types -Helix -Pleated sheet  Mad cow disease -Prion disease -Prions: infectious proteins that become improperly folded -The infectious and normal forms don’t differ in amino acid sequences -Instead, their shapes are radically different -Misfolded proteins make beta pleated sheets  Beta pleated sheets -Cause the misfolded prions to clump up -Causes many diseases, depending on the host -Transmitted by eating tissue contaminated with the prions containing the beta pleated sheets -All of these diseases are fatal  Secondary structure is protein dependent -Not all proteins have both the alpha helix and beta pleated sheets -Some proteins only have one type of secondary structure  Alpha helix only: alpha-keratin, a protein of hair  Beta sheets dominate: silk from spiders Tertiary  Bonding between side chains (R groups) of the various amino acids  R chains provide tertiary structure -Hydrophobic interactions: nonpolar side chains usually cluster at the core of protein (out of contact with water) -Hydrogen bonds between tertiary structure -Ionic bonds between positively and negatively charged side chains -Disulfide bridges (strong covalent bonds) form when 2 cysteine monomers are brought close together by the folding of the protein Quaternary  Interaction of more than one polypeptide chain (or subunit)  Some proteins consist of more than one polypeptide chain -e.g.: transthyretin is an aggregation of 4 subunits Nucleic Acids : store, transmit, and help express heredity information  The amino acid sequence of a polypeptide is programmed by a unit of inheritance called a gene  Genes consist of DNA, a nucleic acid made of monomers called nucleotides Roles of Nucleotides  2 types -Deoxyribonucleic acid (DNA) -Ribonucleic (RNA)  DNA provides directions for its own replication  DNA directs synthesis of messenger RNA (mRNA) and through mRNA, controls protein synthesis  This process is called gene expression  Each gene along a DNA molecule directs synthesis of a mRNA  The mRNA molecule interacts with the cell’s protein-synthesizing machinery to direct production of a polypeptide  The flow of genetic information is DNARNAprotein Components of Nucleic Acids  Nucleic acids are polymers called polynucleotides  Each polynucleotide is made of monomers called nucleotides  Each nucleotide consists of a nitrogenous base, a pentose sugar, and one or more phosphate group  Nucleoside: part of a nucleotide without a phosphate group  Nucleoside=nitrogenous base + sugar  2 families of nitrogenous bases -Pyrimidines (cytosine, thymine, and uracil) have a single six- membered ring -Purines (adenine and guanine) have six-membered ring fused to a five-member ring  In DNA, the sugar is deoxyribose; in RNA, the sugar is ribose  Nucleotide=nucleoside + phosphate group Nucleotide Polymers  Nucleotides are linked together to build a polynucleotide  Adjacent nucleotides are joined by a phosphodiester linkage, which consists of a phosphate group that links the sugars of 2 nucleotides  These links create a backbone of sugar-phosphate units with nitrogenous bases as appendages  The sequence of bases along a DNA or mRNA polymer is unique for each gene Structures of DNA and RNA Molecules  DNA molecules have 2 polynucleotides spiraling around an imaginary axis, forming a double helix  The backbones run in opposite 5’ to 3’ directions from each other, an arrangement know as antiparallel  One DNA molecule includes many genes  Only certain bases in DNA pair up and form hydrogen bonds -adenine pairs with thymine -guanine pairs with cytosine  This is called complementary base pairing  This makes it possible to generate 2 identical copies of each DNA molecule in a cell preparing to divide  RNA: single stranded  Complementary pairing can also occur between 2 RNA molecules or between parts of the same molecule  In RNA, thymine is replaced by uracil, so uracil and adenine pair up  While DNA always exists as a double helix, RNA molecules are more variable in form


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