MBB 222 Lecture Notes - Lecture 10: Conformational Entropy, Protein Folding, Thermodynamics

10 views2 pages

Document Summary

Lecture 10 part 3: proteins - tertiary structure and folding. As soon as the first part of the nascent chain is extruded, it will start to fold co- translationally (i. e. , at the same time as the protein is being synthesized) this segment will acquire secondary structure. In some cases the folded polypeptides will associate with other proteins to form a quaternary structure. Protein folding is usually thermodynamically favorable - g for folding is negative due to a balance of several thermodynamic factors: Conformational entropy ( s): works against folding, since the unfolded protein randomly cycles between many possible states it has a higher entropy value (is more disordered) than the single folded (more ordered) state - s for folding is negative, s<0. Enthalpy contribution ( h): works in favor of folding - formation of energetically favorable interactions - salt bridges, h-bonds, van der waals - between chemical groups in the folded state - h is negative, h<0.

Get access

Grade+
$40 USD/m
Billed monthly
Grade+
Homework Help
Study Guides
Textbook Solutions
Class Notes
Textbook Notes
Booster Class
10 Verified Answers
Class+
$30 USD/m
Billed monthly
Class+
Homework Help
Study Guides
Textbook Solutions
Class Notes
Textbook Notes
Booster Class
7 Verified Answers

Related Documents

Related Questions