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Unformatted text preview: Lecture 4, Wednesday, August 31, 2011 Announcements: 1. re quiz on 9/7: Prof will cut this Friday’s lecture 5 min short, and explain what will be on the quiz next week. (For the rest of this semester, these quiz info sessions will occur in the last 5 minutes of the Monday lectures). 2. Use the Virtual Office Hours! Send e-mail to [email protected] . 3. DO read the first 2 pages of the LG! This gives you basic course info. There is no need to ask the prof for information that is on these pages. Also, no need to e-mail prof re exam conflicts. There will be make-up midterm and make-up final exams. Prof will meet with students when the time draws near and find a suitable day/time. 4. Any interested transfer students (other welcome too!): “How to succeed at this place” Comstock B108 at 2:55PM Friday 9/2. 5. Sunday 9/4 PyMOL tutorial review session in Carpenter Hall Red Room 3 - 5PM. Tu in Malott 251 4:30 - 6PM. 6. CU Block & Bridle Club. Large animal/livestock experience. First meeting of the semester, TODAY Wed 8/31 at 5:30PM in 146 Morrison. 7. CU Food Science Club. First meeting of the semester TODAY at 5:00PM in 404 Plant Science Bldg. **8** BECAUSE OF A SCHEDULING MISTAKE, OFFICE HOURS EACH MONDAY 2 - 4PM WILL BE IN ROOM 402 BIOTECH (NOT 202). Wednesday's lecture: ⋅ We finished discussion of properties of individual AA ⋅ Peptide bond formation ⋅ The hydrophobic effect : water has many ways to H-bond to its neighbors, forming on average 3-4 H-bonds per water at physiological temperatures. In other words, there are many ways for “free” water to have the same energy. Note: many ways → higher probability → more favorable, i.e. higher entropy. But nonpolar groups in water reduce the number of ways for water to H-bond to its neighbors, i.e. fewer ways → less probable → less favorable, lower entropy . Thus, the nonpolar groups tend to get out of the water ("are driven out of water"), thereby reducing the number of waters that have nonpolar groups as neighbors. Today's lecture: p. 34 Our systematic study of the patterns of structure in proteins begins with myoglobin. We are going to follow Mb in several lectures. Mb is a “simple” protein in that it binds oxygen, but has no catalytic activity . By examining myoglobin before studying all of the basic principles of protein structure and function, the reasons for learning the basic principles become more obvious. • Myoglobin has 153 AA, and a molecular weight of about 17,000. • It is found in muscle • Myoglobin stores oxygen. • Myoglobin is the reason that muscle is red. At atmospheric pressure, the concentration of oxygen dissolved in water is about 0.3 mM. However, oxygen bound to myoglobin in the cell has a concentration of up to about 100 mM, since that is the Mb concentration. Myoglobin is required for oxygen storage inside cells....
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- Fall '11