Remodeling of the Folding Free Energy Landscape of Staphylococcal Nuclease by Cavity-Creating Mutations

Biochemistry ◽  
2012 ◽  
Vol 51 (47) ◽  
pp. 9535-9546 ◽  
Author(s):  
Julien Roche ◽  
Mariano Dellarole ◽  
Jose A. Caro ◽  
Ewelina Guca ◽  
Douglas R. Norberto ◽  
...  
Keyword(s):  
Free Energy ◽  
Energy Landscape ◽  
Staphylococcal Nuclease ◽  
Free Energy Landscape ◽  
Folding Free Energy

scholarly journals High-Resolution Mapping of a Repeat Protein Folding Free Energy Landscape

2016 ◽  
Vol 111 (11) ◽  
pp. 2368-2376 ◽  
Author(s):  
Martin J. Fossat ◽  
Thuy P. Dao ◽  
Kelly Jenkins ◽  
Mariano Dellarole ◽  
Yinshan Yang ◽  
...  
Keyword(s):  
Free Energy ◽  
Protein Folding ◽  
High Resolution ◽  
Energy Landscape ◽  
Free Energy Landscape ◽  
Repeat Protein ◽  
High Resolution Mapping ◽  
Resolution Mapping ◽  
Folding Free Energy

scholarly journals Quantifying Nonnative Interactions in the Protein-Folding Free-Energy Landscape

2016 ◽  
Vol 111 (2) ◽  
pp. 287-293 ◽  
Author(s):  
Paulo Ricardo Mouro ◽  
Vinícius de Godoi Contessoto ◽  
Jorge Chahine ◽  
Ronaldo Junio de Oliveira ◽  
Vitor Barbanti Pereira Leite
Keyword(s):  
Free Energy ◽  
Protein Folding ◽  
Energy Landscape ◽  
Free Energy Landscape ◽  
Folding Free Energy

scholarly journals Folding Free Energy Landscape of Ordered and Intrinsically Disordered Proteins

2019 ◽  
Vol 9 (1) ◽  
Author(s):  
Song-Ho Chong ◽  
Sihyun Ham
Keyword(s):  
Free Energy ◽  
Intrinsically Disordered Proteins ◽  
Energy Landscape ◽  
Disordered Proteins ◽  
Free Energy Landscape ◽  
Ww Domain ◽  
Intrinsically Disordered ◽  
Ca 50 ◽  
Folding Free Energy

Abstract Folding funnel is the essential concept of the free energy landscape for ordered proteins. How does this concept apply to intrinsically disordered proteins (IDPs)? Here, we address this fundamental question through the explicit characterization of the free energy landscapes of the representative α-helical (HP-35) and β-sheet (WW domain) proteins and of an IDP (pKID) that folds upon binding to its partner (KIX). We demonstrate that HP-35 and WW domain indeed exhibit the steep folding funnel: the landscape slope for these proteins is ca. −50 kcal/mol, meaning that the free energy decreases by ~5 kcal/mol upon the formation of 10% native contacts. On the other hand, the landscape of pKID is funneled but considerably shallower (slope of −24 kcal/mol), which explains why pKID is disordered in free environments. Upon binding to KIX, the landscape of pKID now becomes significantly steep (slope of −54 kcal/mol), which enables otherwise disordered pKID to fold. We also show that it is the pKID–KIX intermolecular interactions originating from hydrophobic residues that mainly confer the steep folding funnel. The present work not only provides the quantitative characterization of the protein folding free energy landscape, but also establishes the usefulness of the folding funnel concept to IDPs.

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