Bio 151-000

1. Bio 151-000 Academic Coordinator -- Dr. Alma Ferrier Office: Room 216 Thomas Hunt Morgan Building See web site or syllabus for TA and Academic Coordinator contact information. Primary TA: NAME Office Phone #: xxx-xxxx Office Location: Where Located Office Hours: Days and hours Email: email Secondary TA: NAME Email: email

2. Syllabus • Course Description • Bio 151 is the 1st semester of a two semester introductory sequence for life science majors. The companion lecture course is Bio 150. This course is designed to prepare students for upper level Biology • courses. Bio 151 is mainly consists of experimentation in the areas of biochemistry, cell and molecular biology, genetics, and evolution. Students will perform experiments, analyze results, and submit their • observations in the form of lab reports. • Attendance: • Attendance is required in the laboratory section to which you are assigned. Five points will be deducted for each unexcused absence

3. Syllabus • Improper care and storage of microscopes and messes in your work • area will result in a Five-point deduction each time • Plagiarism and Cheating -- Read the section covering this in the • Students Rights and Responsibilities Handbook, University of Kentucky

4. Syllabus Homework For Modules: The homework assignments for modules are a series of worksheets, which you are required to complete during the course of the semester. The homework will consist of questions covering material in the course texts. The assignments may be downloaded from the web site http://www.biology.uky.edu/bio150labs/ Homework must be submitted before the beginning of the class period for which they are due (see syllabus for the exceptions) and which you are officially registered. Late submissions will not be accepted.

5. Syllabus 1. Required Texts: 1. Biology by Neil Campbell, 5th or 6th edition,Benjamin Cummings Publishing Company or a Current Introductory Biology Book. 2. Laboratory Manual Bio 151 7th edition by Doris Westerman

6. Module 1Chemosynthetic Theory and Introduction to Simple Amino Acids

7. Chemosynthetic Theory or “Chemical Evolution": is the abiotic (non-living) synthesis of organic molecules.Organic Molecules are by definition molecules that contain the element carbon. Once thought to come from only living things, organic compounds range from simple molecules such as methane CH4 to colossal ones such as proteins with thousands of atoms. The elements of life which compose these molecules: Carbon Hydrogen Oxygen Nitrogen Phosphorus Sulfur

9. Oparin-Haldane hypothesis (1920s): Primitive Earth’s reducing atmosphere favored chemical reactions that synthesized organic compounds from inorganic precursors present in the early atmosphere and seas. Miller-Urey (1953) tested this hypothesis by: Simulating primitive Earth’s atmosphere with H2O, H2, CH4, CH3, CO, CO2, and N2. Then Exposing this atmosphere to sparks (simulating lightning and providing extreme heat). Observed the formation of organic molecules, including amino acids. Thereby allowing the formation of proteins

10. Figure 26.4  Abiotic synthesis of organic molecules in a model system

11. Amino Acids and Simple Peptides There are 20 common amino acids which are important in protein formation. The R group(side chain) is different for each amino acid and is what gives each amino acid is unique characteristic Of the 20 amino acids, 19 contain asymmetric "-carbons. These 19 amino acids can form isomers. They isomers have been named L and D. The L-form is what is naturally occurring in living systems. The only amino acid that does not have an L and D form is Glycine (It's R-group is a hydrogen atom). Amino Acids are joined by an amide bond known as the peptide bond. When the bond is formed, H2O is liberated

12. Unnumbered Figure (page 68) Amino acid structure

13. Figure 5.15a The 20 amino acids of proteins

14. Figure 5.15b The 20 amino acids of proteins

15. Figure 5.15c The 20 amino acids of proteins

17. Two enantiomers possible for most amino acids L-form found almost exclusively in naturally occurring proteins

19. Assigning Amino Acids as either D or L EXAMPLE: The amino acid alanine is shown below. Bonded to its alpha carbon atom are: a carboxyl group (COO-) an amino group (NH3+) a methyl group (CH3)(its R group) a hydrogen atom

20. Assigning Amino Acids as either D or L If you orient the molecule so that you look along it from the COO- group to the NH3+ group, the methyl (R) group can extend out to the left, forming L-alanine(shown below on the left) or to the right, forming D-alanine (on the right).

21. Polypeptides (proteins) The importance of proteins is implied by their name, which comes from the greek word proteios meaning “first place”. Proteins are the most structurally sophisticated molecules known. Each type having a unique three-dimensional shape or conformation. Polypeptides are formed by the condensation of multiple amino acids forming a polypeptide chain.

22. Figure 5.16 Making a polypeptide chain

23. Formation of a Peptide Activity (10 minutes) • Per Group of Two Gather the Following Materials • three of the stick models that are in the form of a tetrahedron. Each tetrahedron will symbolize one amino acid. • 3 purple, 3 green, 3 white, and 3 red gumdrops. These will be placed on the model to symbolize the different parts of the amino acids. • white gumdrops will symbolize the free hydrogen on the alpha carbon of the amino acid • red gumdrop will symbolize the amino group that is attached to the alpha carbon • purple will represent the carboxyl group • green will represent the R group of the amino acid

24. Formation of a Peptide Activity (5 minutes) • Amino acids combine and displace water to form a peptide bond between the amino group of one amino acid and the carboxyl group of another amino acid (Condensation) • At the cellular level, translation is the process by which polypeptide chains are formed. The N-terminus of an amino acid is joined to the C-terminusof the previous amino acid forming a peptide chain. • Now, join your three amino acids, one at a time to displace one molecule of water, forming a peptide bond between each amino acid.

25. Now that you have made polypeptide, what type of characteristics do these chains exhibit that produce unique properties to their structure and function? Read Chapters 1-5 in Campbell and be prepared to discuss this question next class.

26. RASMOL Next class, you will perform some computer exercises during class. You may download these exercises from the website at www.biology.uky.edu/bio150labs . Be sure to See if you can down load the assignment as it will be due next week.

27. Final Slide