Biology 1001A Lecture 3: Topic 3.docx

27 views6 pages

Document Summary

Proteins are linear polymers of amino acids but get crunched and fold 50 to > 30,000 amino acids. Condensation reaction (bonding of two amino acids result in water molecule) Partial double bond character due to resonance structure (planar structure which effects the rotation of the polypeptides and the folding of the protein) (atoms involved are coplanar) Restricted rotation on n=c but free rotation on c-r. Residues: the remaining part of amino acids (minus water) after condensations. This defines what the rest of the protein is going to look like. Secondary structure is considered local folding because it is created by the backbone only, stabilized by hydrogen bonds in backbone (c=o) and alpha amino group (n-h) (side chains are not involved at all). Two main type of second structure: alpha helix, beta helix: make up about 50% of protein. Alpha helix: coil spring arrangement, side chains project outwards (no interior space, h-bond stabilization.

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 Documents

Related Questions