Biochemistry Online: An Approach Based on Chemical Logic

Biochemistry Online

CHAPTER 2 - PROTEIN STRUCTURE

D:  PROTEIN FOLDING AND STABILITY

BIOCHEMISTRY - DR. JAKUBOWSKI

Last Update:  3/1/16

Learning Goals/Objectives for Chapter 2D:  After class and this reading, students will be able to

  • differentiate between thermodynamic (equilibrium) and kinetic (timed) approaches to the study of protein folding reactions
  • describe techniques to study transient (kinetic) and long-lived (thermodynamic) intermediates in protein folding
  • describe the following intermediates in protein folding:  molten globule, X-Pro isomers; Disulfide bond intermediates
  • interpret spectral and chromatographic data from protein folding studies and use this to determine or explain a mechanism for folding
  • describe properties of folded, unfolded, molten globule, and intrinsically disordered proteins
  • explain the difference between the environments for protein folding when performed in vitro and in vivo
  • state the role of molecular chaperones in in vivo protein folding
  • describe differences in disulfide bond occurrence in cytoplasmic and extracellular proteins

D1.  Introduction

D2.  Protein Folding In Vitro

D3.  Folding of Single Protein Molecules

D4.  The Denatured State

D5.  Multiple Conformations from The Same Sequence

D6. Protein Folding In Vivo

D7.  Redox Chemistry and Protein Folding  

D8.  Protein Transport Across Membranes

D9.  Recent References

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Biochemistry Online by Henry Jakubowski is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License.