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Bio 002 Exam 2

by: Jennifer Mendoza

Bio 002 Exam 2 BIO 002

Jennifer Mendoza

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I took most notes from his lecture slide. Although I do recommend to read the book, review the h/w and go over his in class worksheets. There was a lot of information to cover, so hopefully this se...
Dr. Kamal Dulai
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This 8 page Study Guide was uploaded by Jennifer Mendoza on Sunday October 16, 2016. The Study Guide belongs to BIO 002 at University of California - Merced taught by Dr. Kamal Dulai in Fall 2016. Since its upload, it has received 107 views.

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Date Created: 10/16/16
Exam 2 Fast Review *If in red really important *If highlighted pay *If left simple look at it, and attention to it look it up on google if you don’t already know what that is or means. Ch. 1 and 2  Know animal and plant cell o Differences and similarities  Prokaryote vs Eukaryote o Eukaryotic cells have organelles and prokaryotic don’t  Know metric system o Ex. 1 meter= 10^9 nm Test will consist about 1/3 of Ch.  Know your different bonds 1and 2. As said by o Covalent, hydrogen and iconic the professor. o Polar and nonpolar bonds  Review Functional groups and isomers  Remember Cell Theory ***** The following Chapters 11, 3, 4 and 5 will be 2/3 of the exam. ***** Ch. 11 Membrane Organization and Function  Membrane structure o Also known as plasma membrane, Cell membrane, lipid bilayer and membrane  No cell on earth can exist without a cell membrane o No membrane= no cells= no life  A cell membrane is 50 atoms thick= 5nm  Know the membranes function o What is it there for? o Why is it important? o What does it does it work?  Piercing of the cell membrane does not cause for it to pop or tear. It simply reseals! o No Edges  Any tears are quickly repaired by either  The exclusion of the water molecules  The formation of small vesicles  No Free Edges are permitted by the free energy of the system  Therefore, the only way a large collection of these membranes can exist without edges is as sacs- exactly what the plasma membrane is!  Bacteria only has one membrane- plasma membrane  Eukaryotes have many internal membranes too- these offer each organelle the ability to concentrate certain chemicals.  All natural membranes are made of lipids and proteins.  The character of the membrane can change, and the natural membranes are rarely found without accompanying proteins. The Lipid Bilayer o Lipid molecule contains two distinct properties  Hydrophilic head and one or two hydrophobic tails o Most abundant lipids= phospholipids – the head is linked to the rest of the molecule through ta phosphate group. o Phosphatidylcholine is the most abundant of all  Hydrophilic head- loves water- polar- Choline, phosphate and glycerol Hydrophobic tails- doesn’t like water- nonpolar- has a double bond- two long hydrocarbon chains  Amphipathic nature  The lowest energy structure which is formed by amphipathic molecules is a lipid bilayer.  No flip-floppers please o A single lipid molecule will rarely flip form one surface of the molecule to the other- no flip-flopping- Mr. Dakaucas o Lipid molecule is free though to move within its own layer relatively freely o Spin at RT about 30,000 rpm on their axis- like spinning tops.  Lateral diffusion ----  Flip- flop (rarely occure) Saturated Fats  Properties of different membranes dictated by their composition o Length of hydrocarbon tail (14 to 24 carbon atoms- the shorter the more fluid) o Saturated- single bonds all the way down, and more rigid  Ex. Butter o Unsaturated- double bond between two carbons, and is more fluid  Ex. Oil  Hydrogenated margarines  Cholesterol= more rigid membrane- bad  The membrane is asymmetrical  Flippases- enzymes- which permit the manufacture of asymmetric lipid membranes  New membrane made only by the ER  Scramblases- Know where it happens Membrane Proteins 1. Describe the 4 classes of membrane proteins found in cell membranes 2. Differentiate between integral and peripheral membrane proteins 3. Compare and contrast the different anchoring mechanisms used to prevent membrane proteins from migrating 4. Differentiate between apical, lateral or basal sides of cells 5. Compare paracellular and transcellular transport Ch. 3 Energy Catalysis Biosynthesis What to know? st nd 1. Define the 1 and 2 law of thermodynamics 2. Understand how enzymes influence chemical reactions 3. Describe energy coupling 4. Define energy carriers 5. Compare and contrast Biosynthetic pathways Ch. 4 Protein Structure and Function What to know, review and pay close attention to? 1. Describe how the shape and structure of a protein is determined 2. Know the differences between a polypeptide and protein 3. List the main 9 functions of proteins 4. Compare and contrast the properties of the 20 common amino acids 5. Describe the classes of proteins based on structure 6. Compare the common folding patterns of proteins- alpha-helices and beta sheets 7. Describe an unstructured region of a protein 8. Define protein families 9. Compare monomer vs. multimeric proteins 10. Understand how proteins are stabilized 11. Describe the common (and not so common) ways that proteins are regulated 12. Compare the methods via which proteins are studied Note while in class on this chapter: Outline for this Ch. Protein  Proteins are major components Wow!!! Facts of ALL cellular systems  Proteins consist of one or more LINEAR polymers called PLYPEPTIDES  Proteins are LINEAR and NEVER branched  Different AA's are linked together via PEPTIDE BONDS  The individual amino acids within a protein are known as RESIDUES  Simple The smallest known P' is just understanding NINE(9) residues long- OXYTOCIN of protein  The largest is over 25,000…  structure Proteins are GENERALLY between 50 and 2000 -1 primary sequence  Amino acids are put together by polypeptides???- google  Ribosomes are the only structures that can make proteins other than us in the lab.  They are told what to make by messenger RNA  The original information comes from DNA  DNA --> mRNA--> ribosomes  Amino acids (20)--> 10 are hydrophobic and 10 hydrophilic o For the 10 hydrophilic- 2(-), 2(+) and 5(&+)  Ribosome produces polypeptides into the cytoplasm  The gene determines in what order the amino acid will be placed.  Ionic or covalent bonds are made in different polypeptides to act as a molecular staple. -2 secondary structure  The final shape the protein takes up is determined by the primary steps.  Hydrogen bond between atoms of two polypeptide bonds.  In some cases a protein can change shape due to the environment in which it exist- (protein is denatured)  Post- translations:???-google  When you make a protein it can be further modified by the chemistry of the cell.  Shape determines function!  Alpha helix and beta helix - these helixes can be left or right handed o Ex. DNA is right handed helix  Different proteins are made by different polypeptides placed in a different place -3 Tertiary Structure  Tertiary Structure- For most proteins the final level of organization. Functions protein consist of just one polypeptide chain.  Miracle of Evolution- This protein is the structure of an anti-freeze developed by Nature over 500 million years ago.  The blue dots in conjunction with the beta sheets…  Green spirals alpha helixes.  Domain- region of a protein that is highly structured; reproducible structures; have no structure. o They can be classified at different levels:  Alpha helix green spiral, beta sheet white string and red arrows  Polypeptides  Super domains, protein of molecules  Elastase is found in your skin  Chymotrosipn- bind proteins in digestive tract. -4 Quaternary Structure  MULTImeric-AAAA, AABB and AABC  IN SOME CASES Nature has decided to REUSE the same polypeptides as monomers…  A A or A-B  Held together by ionic or covalent bonds Allosteric  Oher (Allo)  Steric (site)  Ex. A car has a driver's seat, if you take a wheel off you can’t drive anymore, but you can put it back on and the car will work again  Something that drives an activity Ch. 5 What you should know? 1. Describe the structure of nucleosides, nucleotides and other small molecules nucleotides in a cell. 2. Illustrate the complementary nature of the DNA molecule. 3. Describe the structure of chromosomes. 4. Understand the definition of genome. 5. Define the role played by non-coding DNA regions, such as centromeres, OIRs and Telomeres. 6. Describe how chromosomes structure is related to function. 7. Define the nature of nucleosome structure and function. 8. List the different orders of chromatin packaging 9. Explain chromatin remodeling 10. Compare and contrast Heterochromatin and euchromatin. 11. Explain chromosome silencing. Hope this can help you prepare for the exam. Most of it was taken from his lecture notes, but do not limit your studies to just that make sure to read the text, REVIEW THE H/W and look at his in class worksheet!


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