Class Notes (835,529)
Canada (509,225)
York University (35,236)
Biology (2,238)
BIOL 2020 (116)
K Wheaton (5)
Lecture

chapter 8 textbook notes.docx

1 Page
68 Views
Unlock Document

Department
Biology
Course
BIOL 2020
Professor
K Wheaton
Semester
Fall

Description
Hemoglobin an allosteric protein 8.1 hemoglobin displays cooperative behaviour  Hemoglobin has a sigmoidal curve 8.2 Myoglobin and hemoglobin bind oxygen in heme groups  Myoglobin, single polypeptide, tertiary structure, composed of alpha helices, globin fold (holds them together)  Heme gives muscle and blood its distinctive red color  consists of 4 pyrrole rings linked by methane bridges  Hemoglobin has yielded the basis for observing the brain in action 8.3 Hemoglobin binds oxygen cooperatively  Hemoglobin  quaternary structure, tetramer, alpha beta dimmers  When going from T to R, the 5 coordination site histidine moves with the iron ion 8.4 An allosteric regulator determines the oxygen affinity of hemoglobin  The interaction is facilitated by ionic bonds between the negative charges on 2, 3- BPG and three positively charged groups of each beta chain  Mutation of sickle cell: reduces the solubility of the deoxygenated but not teh oxygenated form of hemoglobin, therefore sickling results w
More Less

Related notes for BIOL 2020

Log In


OR

Join OneClass

Access over 10 million pages of study
documents for 1.3 million courses.

Sign up

Join to view


OR

By registering, I agree to the Terms and Privacy Policies
Already have an account?
Just a few more details

So we can recommend you notes for your school.

Reset Password

Please enter below the email address you registered with and we will send you a link to reset your password.

Add your courses

Get notes from the top students in your class.


Submit