scholarly journals High-Resolution Free-Energy Landscape Analysis of α-Helical Protein Folding: HP35 and Its Double Mutant

2013 ◽  
Vol 9 (12) ◽  
pp. 5257-5266 ◽  
Author(s):  
Polina V. Banushkina ◽  
Sergei V. Krivov
2016 ◽  
Vol 111 (11) ◽  
pp. 2368-2376 ◽  
Author(s):  
Martin J. Fossat ◽  
Thuy P. Dao ◽  
Kelly Jenkins ◽  
Mariano Dellarole ◽  
Yinshan Yang ◽  
...  

2015 ◽  
Vol 43 (2) ◽  
pp. 157-161 ◽  
Author(s):  
Polina V. Banushkina ◽  
Sergei V. Krivov

The free energy landscape can provide a quantitative description of folding dynamics, if determined as a function of an optimally chosen reaction coordinate. The profile together with the optimal coordinate allows one to directly determine such basic properties of folding dynamics as the configurations of the minima and transition states, the heights of the barriers, the value of the pre-exponential factor and its relation to the transition path times. In the present study, we review the framework, in particular, the approach to determine such an optimal coordinate, and its application to the analysis of simulated protein folding dynamics.


Nano Letters ◽  
2019 ◽  
Vol 19 (9) ◽  
pp. 6442-6453 ◽  
Author(s):  
Estefania Mulvihill ◽  
Moritz Pfreundschuh ◽  
Johannes Thoma ◽  
Noah Ritzmann ◽  
Daniel J. Müller

Biochemistry ◽  
2017 ◽  
Vol 56 (31) ◽  
pp. 4053-4063 ◽  
Author(s):  
Pooja Malhotra ◽  
Prashant N. Jethva ◽  
Jayant B. Udgaonkar

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