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Principles of Physics

Much of what happens in our bodies is affected not only by biological principles but those of physics, chemistry and mathematics. Principles of Physics. Inverse Square Law.

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Principles of Physics

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  1. Much of what happens in our bodies is affected not only by biological principles but those of physics, chemistry and mathematics Principles of Physics Inverse Square Law This is where the gravitational force between any two bodies varies directly as the product of their masses and inversely as the square of the distance between them. Formula : F = G ( m1m2) d 2
  2. Origins of the Inverse Square Law
  3. Pieces of the puzzle According to what you read, what are the values for d, F, m and G ? d = distance between the centers of the spherical masses (meters) F = net force (newtons) m = mass (Kilograms) -11 G = universal constant = 6.67 X 10 N Revaluate what you have done in working with the assigned problems. Be sure to check that you are using the correct units.
  4. Principles of Physics Electrostatics: The study of electrical charges that can be collected and held in one place. What are the types of charges and how are they represented? What is the natural charge of an atom? Describe the structure With the addition of energy electrons can be removed from atoms. … if this occurs how is the atom changed? Electrons can be transferred but individual charges are neither created nor destroyed If an electron transfer occurs between two objects the total charge of the two objects remains the same, it is conserved
  5. http://workbench.concord.org/database/activities/157.html - overview Click on “go to activity” (This may take a few minutes so be patient) Manipulate the charges on the screen to see how the yellow molecules are effected. How must you manipulate the charges to get all of the yellow molecules to go (and stay) on the left? 2. Does the amount of charge affect the time it takes to get all of the molecules to stay to the left of the screen? 3. Can you get all of the molecules to stay to the left even with the addition of a negative charge? Explain your answer 4. Starting with all of the green molecules at a +5 charge choose a spot to put 6 consecutive charges of -5. Then, do the same, but space the – 30 charge out over the green molecules instead of in one place. In which scenario were you able to more effectively get more yellow molecules to the right side of the field? Explain why.
  6. Effect of Electrostatic Interactions on Folding Now that you have manipulated charges to view their attractive and repellant properties based on charge we will look at how these charges can effect the folding of a protein Go to http://workbench.concord.org/database/activities/213.html Click on “go to activity” Using the worksheet provided investigate protein folding and answer the questions provided
  7. Bioinformatics: Protein Folding Name: ______________________ Pd:_____ http://workbench.concord.org/database/activities/213.html Once the page is loaded play both the original chain and the alternately charged chain. Change arganine to lysine on the last three red arganine molecules and then skip three more arganine from the end and change the next three (the 7th, 8th and 9th molecules from the end of the chain) to lysine as well. 1. How does this change the protein formation? Why? Reset the model Change arganine to aspartic acid on the last three red arganine molecules and then skip three more arganine from the end and change the next three (the 7th, 8th and 9th molecules from the end of the chain) to aspartic acid as well. 2. How does this change the protein formation? Why? Do not reset the model Now change the first 6 of the arganine chain ( the ones closest to the glutamic acid chain ) to valine. 3. How does this change the protein formation? 4. Which change (arganine to aspartic acid or arganine to valine) do you believe caused the biggest change in the folding of the protein? Why? Go to: http://cnx.org/content/m11467/latest/ Read the introduction and the section titled misfolding 5. What is the importance of protein folding on protein function?
  8. Coulomb’s Law
  9. Coulomb’s Law Coulomb's law, sometimes called the Coulomb law, is an equation describing the electrostatic force between electric charges. It was developed in the 1780s by French physicist Charles Augustin de Coulomb and was essential to the development of the theory of electromagnetism. Coulomb's law may be stated in scalar form as follows: The magnitude of the electrostatic force between two pointelectric charges is directly proportionalto the product of the magnitudes of each of the charges and inversely proportional to the square of the total distance between the two charges. Formula : F = K ( q q’) d 2
  10. Pieces of the Formula F = K ( q q’) d 2 Where F = force (newtons) K = 9.0 x 10 N x m / C (when charge is in coulombs, distance in meters and force in newtons) q = charge 1 (coulombs) q’ = charge 2 (coulombs) d = distance between charges 1 and 2 (meters) 9 2 2
  11. Go to the following web site and read the background information provided. Then answer questions 1 to 7 in your notes. Be sure to show your work. http://www.physicsclassroom.com/Class/estatics/U8L3b.cfm Then, complete numbers 6 to 13 in the text copy provided, for tomorrow (page 423)
  12. Chemical Bonding A chemical bond is a mutual electrical attraction between the nuclei and valence electrons of different atoms that binds the atoms together. Chemical boding occurs due to redistribution of valence electrons in ways that make the atoms more stable. We will investigate the different types of chemical bonding. There are two major categories: ___________________ Ionic Bonding where one atom completely “gives up” electrons to another atom 2. ____________________ Covalent Bonding where two atoms “share” electrons.
  13. Covalent bonding has two categories: There is an even distribution of charge (electrons are shared equally) 1. Nonpolar- covalent 2. Polar-covalent There is an uneven distribution of charge (electrons are not shared equally) Today you will investigate the different types of chemical bonding and how their electronegativity can be used to predict the type of bond present between two given atoms Go to the web site below beginning with page one work your way through the tutorial and answer the questions provided as you go. http://mw2.concord.org/public/part2/bondtype/page1.cml http://workbench.concord.org/database/activities/235.html
  14. Review Topics we have covered: inverse square law Electrostatics Charges Polarity non-polar covalent bonds polar covalent bonds ionic bonds dipole-dipole forces london dispersion forces coulomb’s law protein folding
  15. Answer the following questions to review some of the concepts we have covered. Object A has a positive charge of 6.0 x 10 C. Object B carrying a positive charge of 3.0 x 10 C is 0.030 m away. a) Calculate the force on A b) What would be the force if the charge on B were negative? 2. If one object has a mass of 70.0Kg and a second has a mass of 50.0Kg and they are a distance of 20.0 m apart what is the value of the force? 3. If the difference in electronegativity is 2.7 between two atoms what kind of bond do they share? 4. Does charge effect the ability of a protein to fold correctly? If so is this a problem? Explain. 5. What is the difference between an ionic and a covalent bond? 6. Develop 6 questions concerning this material. Place the questions at the top of the page and the answers to these questions at the bottom of the sheet. Use the web pages we have used and any worksheets or notes we’ve taken to help you in your question creation. If you develop a good question perhaps it will be on your next exam…
  16. Some web addresses we have used….. http://workbench.concord.org/database/activities/157.html - overview http://workbench.concord.org/database/activities/213.html http://www.physicsclassroom.com/Class/estatics/U8L3b.cfm http://mw2.concord.org/public/part2/bondtype/page1.cml http://workbench.concord.org/database/activities/235.html
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