BIO206H5 Lecture Notes - Lecture 4: Protein Folding, Hydrophile, Hemoglobin

28 views4 pages
30 Oct 2016
School
Department
Course

Document Summary

The linear sequence of protein sequence n-terminal to c-terminal. Typically finding proteins ranging in size from 50 amino acids to over 2000 amino acids. Single letter abbreviations for the amino acids as well for instance, cysteine is c or cys (three letter abbreviation) Chemical properties of amino acids that give the biological and chemical properties of proteins. The primary sequence of amino acids could have an effect of a single change which may be huge. For instance, hemoglobin and sickle-cell anemia at position #6 there should be a glutamic acid but if it substitutes to a valine, it causes sickle cell anemia. Arrangement (folding pattern) of small portions of the polypeptide backbone. Look at certain segments of the polypeptide chain that fold into regular patterns. Most common structures: alpha helix and beta-pleated sheet (strands) Other structures: turns, nonrepeating (loops and coils)

Get access

Grade+20% off
$8 USD/m$10 USD/m
Billed $96 USD annually
Grade+
Homework Help
Study Guides
Textbook Solutions
Class Notes
Textbook Notes
Booster Class
40 Verified Answers
Class+
$8 USD/m
Billed $96 USD annually
Class+
Homework Help
Study Guides
Textbook Solutions
Class Notes
Textbook Notes
Booster Class
30 Verified Answers

Related textbook solutions

Related Documents

Related Questions