"Wet" Versus "Dry" Folding of Polyproline
Liuqing Shi1, Alison E Holliday2, Brian C Bohrer3
1Department of Chemistry, Indiana University, Bloomington, IN, 47405, USA.
Journal of the American Society for Mass Spectrometry
|April 10, 2016
Summary
Polyproline helices transition between PPI (all-cis) and PPII (all-trans) forms. Solvent-free intermediates refold efficiently into PPI, revealing conserved folding pathways in both solution and vacuum, highlighting water
Area of Science:
- Chemical Physics
- Biophysical Chemistry
- Polymer Science
Background:
- Polyproline helices exist in two main forms: the all-cis polyproline-I (PPI) and the all-trans polyproline-II (PPII) helix.
- The transition between PPI and PPII is influenced by solvent conditions, with PPI favored in 1-propanol and PPII in water.
- Previous studies identified at least six intermediates during the PPI to PPII transition in aqueous solution.
Purpose of the Study:
- To investigate the refolding pathways of PPI-water intermediates in a solvent-free environment.
- To compare the folding mechanisms in solution versus in vacuo.
- To elucidate the role of water in stabilizing specific polyproline conformations.
Main Methods:
- Utilizing solvent-free intermediates generated from the PPI to PPII transition.
- Employing collisional activation in a vacuum to induce refolding.
- Analyzing refolding pathways using principles observed in solution-phase transitions.
Main Results:
- Solvent-free intermediates refold into the PPI helix with high efficiency (>90%).
- The refolding pathways in a solvent-free environment mirror those observed in solution.
- Gentle activation conditions allow some PPII-like structures to form PPII even in a vacuum.
Conclusions:
- The PPI helix is favored under dry conditions, underscoring water's role in promoting the trans proline preference.
- Folding pathways are remarkably conserved between solution-phase (water/propanol) and gas-phase (in vacuo) transitions.
- 1-propanol acts as a mimic of a "dry" environment for polyproline helix folding.
Related Concept Videos
Protein Folding
130.1K
Overview
130.1K
Protein Folding
12.3K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
12.3K
Protein Folding
36.4K
36.4K
Molecular Chaperones and Protein Folding
20.7K
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
The...
20.7K
Molecular Chaperones and Protein Folding
15.5K
15.5K
Protein Folding Quality Check in the RER
5.5K
ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
5.5K


