Foundations of Biology 1
Foundations of Biology 1
Popular in Course
Popular in Biological Sciences
This 3 page Reader was uploaded by David Lee on Sunday August 24, 2014. The Reader belongs to a course at University of Pittsburgh taught by a professor in Fall. Since its upload, it has received 127 views.
Reviews for Foundations of Biology 1
Report this Material
What is Karma?
Karma is the currency of StudySoup.
You can buy or earn more Karma at anytime and redeem it for class notes, study guides, flashcards, and more!
Date Created: 08/24/14
9613 The UreyMiller Experiment resulted in the creation of amino acids and other organic molecules We can synthesize these molecules easily in the lab using other methods What is the deeper significance of these particular results gt In their experiment they created these amino acids and organic molecules using the environment in which the early Earth without life is believed to have proving that life could have started from these environment Why are we learning about chemical evolution in the first place What are the implications when it comes to modern life gt It is important to understand chemical evolution because we can begin to understand more and more why and how certain chemical reactions occur both in the outside world and even within our own bodies Understanding these reactions open up so many more doorways into different fields such as medicine or simply any form of scientific research By understanding these reactions we as a species can come to understand the ways in which to complement or even counteract such reactions in order to better our general lives gt All cells are theoretically chemically related Complex primordial soup Robert with all of the molecules of life some assembling into polymers Criteria for early life gt Sef repication gt Transfer information from one quotgeneration to another gt Subject to natural selection and adaptation to environment What do our earlylife molecules need to do to sef repicate gt They must be able to control catalyze chemical reactions gt They must be able to contain store rudimentary information gt They must be able to reproduce that information somewhat faithfully Chemical evolution gt In natural selection an organism that can reproduce most successfully has an advantage over others of its kind Candidates for first sef repicating molecules gt Early lipids proteins sugars nucleic acids gt Proteins and RNA tend to be main candidates gt RNA world hypothesis RNA is best candidate for being the first sef repicating molecule Proteins primary structure gt Students should understand the critical role proteins play in cells from structural to enzymatic functions and apply concepts from previous chapters to predict and explain the effects of alterations of protein structure on protein function gt Focus I Polar vs nonpolar vs ionic side chains effects in water I Polymerization via dehydration an endergonic reaction I The peptide bond of primary structure General rule gt Most large biological molecules proteins carbohydrates nucleic acids are polymers gt Biological polymers are all built using the same basic chemical reaction 9613 For Polymerization Reaction diagram check powerpoint for this lecture gt Dehydration reaction condensation reaction How a majority of organic macromolecules are built up Endergonic For Depolymerization Reaction diagram check powerpoint for this lecture gt Hydrolysis reaction How a majority of organic macromolecules are broken down Exergonic Common properties of every protein Each unit of a protein is a string Each string is a polymer Each polymer is made up of monomers A protein monomer is an amino acid Monomers are joined by peptide bonds Side note Carboxyl groups are acids Protein properties are dependent on the side chains or the R group Just as functional groups modify organic molecules in general and change their properties so to the R groups of amino acids for the same reasons Side Note The book groups the 20 amino acids by the general properties of their side chains Polymerization is caused by Condensation and Dehydration Which amino acid is more likely to interact with water gt Leucine Valine Threonine or Phenylalanine gt Threonine has unlike the other amino acids whose r groups are generally formed with hydrocarbons which form only non poar bonds an OH molecule attached to its Rgroup which is polar because the electronegativity between the O and H is high gt Side Note A ring in a structural formula is Carbon What best summarizes the relationship between hydrolysis and dehydration reactions gt Dehydration reactions create polymers while hydrolysis breaks them down A single change in primary structure can lead to big change Glutamate is acidic and hydrophilic The R group attached to glutamate is a carboxyl group which is acidic Valine is nonpolar and hydrophobic because the R group consists of hydrocarbons which do not react with water and are therefore hydrophobic and are also known to be nonpolar A single change in primary sequence can lead to huge effects on structure gt For example Valine being hydrophobic hides from water by interacting with other hydrophobic regions causing hemoglobin molecules to clump I Therefore blood cells are distorted and lose elasticity Sickle Cell Disease Poymerization Reaction Diagrams Check Powerpoint for this lecture Primary structure of proteins gt A protein is a string of amino acids held together by very strong covalent bonds gt While heat can destroy them It takes far more heat than is ever produced by human cells Protein primary structure is basically impervious to everything except for hydrolysis enzymes gt Proteins are built in only one direction Ngt C I Connections Genes are also copied and read in only one direction What do structures have in common gt They are entirely based on interactions between amino acids gt Most of these interactions are weak VVVVVV O 00 o 0 9613 Hydrogen bonding Ionic bonding Van der waals interactions One exception disulfide bridges Primary structure versus Secondary Tertiary Quaternary structure gt Primary Directly encoded by DNA Held together by strong covalent peptide bonds String linear shape Broken down only by enzymes Damage irreversible gt Others Dependent on primary structure Held together mostly by weak bonds Three dimensiona shapes Damaged by anything that disrupts weak bonds Damage often reversible Secondary structure gt Universally common protein folding motifs gt Nearly every protein has one or the other pattern Alpha helix or Beta pleated sheet See Powerpoint gt Held by hydrogen bonds between the LIKE portions of amino acids not Rgroups Tertiary structure gt Interactions between R group gt Mostly weak interactions gt Highly diverse shapes gt Dependent upon primary structure Quaternary structure gt Multiple strings forming a larger functional unit gt Some proteins are only one string these don t have quaternary structure
Are you sure you want to buy this material for
You're already Subscribed!
Looks like you've already subscribed to StudySoup, you won't need to purchase another subscription to get this material. To access this material simply click 'View Full Document'