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Study Session from First Exam

by: Elizabeth Notetaker

Study Session from First Exam BIO 160

Marketplace > University of Tennessee - Knoxville > Biology > BIO 160 > Study Session from First Exam
Elizabeth Notetaker

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About this Document

These notes were from a study discussion with Dr. P before our first exam.
Cellular and Molecular Biology
Purnima D Pinnaduwage (P)
Class Notes
cells, Macromolecules
25 ?




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This 2 page Class Notes was uploaded by Elizabeth Notetaker on Friday September 23, 2016. The Class Notes belongs to BIO 160 at University of Tennessee - Knoxville taught by Purnima D Pinnaduwage (P) in Fall 2016. Since its upload, it has received 12 views. For similar materials see Cellular and Molecular Biology in Biology at University of Tennessee - Knoxville.


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Date Created: 09/23/16
 Don’t memorize amino acids structure—just know how to identify  Some questions are recalling info, some are analytical  Look at learning objectives for each chapter  Will not have to write functional groups, but need to know them if you look at them  Know aldehyde and ketone  Is the functional group in sugars, is it hydrophilic/phobic, is it acidic or basic (all according to functional groups)  Polar=hydrophilic and nonpolar=hydrophobic  Know that water has a lot of hydrogen bonds—know that but don’t worry as much about specific properties  Know how to figure out pH from h+ concentration or h+ from pH  pH of 2 to pH of 6 is 10^4  Know acidic or basic of amino acid by R group  Acid is proton donor and base is a proton acceptor (is it is positive, it has accepted a proton OR if it is negative, it has lost an electron)  Look at big picture 6.4 at the end of chapter 6 for comparison of macromolecules (pg 104)  Know structure of amino acid (identify)  Secondary protein structure is H bonds between amine and carboxyl  Tertiary protein structure when R groups interact (hydrophilic, hydrophobic, disulfide bonds, ionic bonds) ONLY in tertiary  Interactions of tertiary structures are easy to break because they’re interactions, so is secondary, but primary is much harder to break so with denaturation usually everything is gone except primary.  Enzymes have active sites that substrate can bind to. They have a lot of interactions with the substrate so they are good catalysts. They can form many different functional groups, active groups, and shapes to interact with substrate.  Proteins have so many different functions because of the structure— they can form many different shapes  Look at notecard questions—will be FBI questions like worksheets  RNA can do more because it has a functional group (-OH) (DNA just has H)  RNA has complementary base pairing with the same strand (looks like light bulb and the pairing is done at the base)  DNA is too stable, double stranded, and nonreactive/functional group, backbone is sugar phosphate compared to RNA.  RNA is in between DNA and protein—some storage and some functional.  Will have a flow chart with all biomolecules  Carbs are very hydrophilic because they have so many hydroxyl groups  Up oxygen equals beta  Down oxygen equals alpha  WILL NEED TO KNOW ALPHA AND BETA FOR THAT  Know where it is linked—which carbon is it using?  Carbon one is the carbon after the ring oxygen  Hydroxyl at top equals beta  Hydroxyl at bottom is alpha  Alpha and beta depend only on the C 1 involved carbon  MUST start with C 1  Three ways monosaccharides differ from each other: -the location of their carbonyl group -the number of carbon atoms they contain -the orientations of their hydroxyl groups  More potential/stored energy in equally shared electrons (C-C and H-H)  Probably will have more questions on chapter 6 since we spent more time on it  Lipids are the most hydrophobic because there are more C-C and C-H bonds  Fats, lipids, steroids  Fats have glycerol and three FA tails—know saturated and unsaturated  Think about each biomolecule in flow chart  PL are amphipathic because glycerol and FA tails are hydrophobic and P group is hydrophilic.  Steroids—cholesterol is a component in animal membranes  Fatty acids (saturated vs unsaturated) and look at increasing chain length and what that does  Look at lipid worksheet  More hydrophobic interactions make it harder to separate  Transport—passive and active chart  Something on osmosis similar to bag question from worksheet  Some questions will be different wordings of worksheets  Difference between channel and carrier—hole vs binding and shape change  If protein is interacting with the membrane it is a hydrophobic protein.  Know one word of function of each organelle to be able to use in a question—ribosomes make lipids is false


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