scholarly journals Using Bayes formula to estimate rates of rare events in transition path sampling simulations

2015 ◽  
Vol 143 (13) ◽  
pp. 134121 ◽  
Author(s):  
Pierre Terrier ◽  
Mihai-Cosmin Marinica ◽  
Manuel Athènes
Keyword(s):  
Rare Events ◽  
Path Sampling ◽  
Transition Path ◽  
Transition Path Sampling ◽  
Bayes Formula

scholarly journals Transition path sampling of rare events by shooting from the top

2017 ◽  
Vol 147 (15) ◽  
pp. 152716 ◽  
Author(s):  
Hendrik Jung ◽  
Kei-ichi Okazaki ◽  
Gerhard Hummer
Keyword(s):  
Rare Events ◽  
Path Sampling ◽  
Transition Path ◽  
Transition Path Sampling

Improved transition path sampling methods for simulation of rare events

2008 ◽  
Vol 128 (14) ◽  
pp. 144104 ◽  
Author(s):  
Manan Chopra ◽  
Rohit Malshe ◽  
Allam S. Reddy ◽  
J. J. de Pablo
Keyword(s):  
Sampling Methods ◽  
Rare Events ◽  
Path Sampling ◽  
Transition Path ◽  
Transition Path Sampling

Rare event simulation

2017 ◽  
Author(s):  
Michael P. Allen ◽  
Dominic J. Tildesley
Keyword(s):  
Rare Event ◽  
Path Sampling ◽  
Rapid Progress ◽  
Computationally Efficient ◽  
Transition Path ◽  
Transition Path Sampling ◽  
Event Simulation ◽  
Reaction Coordinates ◽  
Simulation Techniques ◽  
Transition Interface

The development of techniques to simulate infrequent events has been an area of rapid progress in recent years. In this chapter, we shall discuss some of the simulation techniques developed to study the dynamics of rare events. A basic summary of the statistical mechanics of barrier crossing is followed by a discussion of approaches based on the identification of reaction coordinates, and those which seek to avoid prior assumptions about the transition path. The demanding technique of transition path sampling is introduced and forward flux sampling and transition interface sampling are considered as rigorous but computationally efficient approaches.

scholarly journals Catalytic Mechanism of Processive GlfT2: Transition Path Sampling Investigation of Substrate Translocation

ACS Omega ◽  
2020 ◽  
Vol 5 (34) ◽  
pp. 21374-21384
Author(s):  
Pavel Janoš ◽  
Igor Tvaroška ◽  
Christoph Dellago ◽  
Jaroslav Koča
Keyword(s):  
Catalytic Mechanism ◽  
Path Sampling ◽  
Transition Path ◽  
Transition Path Sampling

Understanding rare safety and reliability events using transition path sampling

2018 ◽  
Vol 108 ◽  
pp. 74-88 ◽  
Author(s):  
Ian H. Moskowitz ◽  
Warren D. Seider ◽  
Amish J. Patel ◽  
Jeffrey E. Arbogast ◽  
Ulku G. Oktem
Keyword(s):  
Path Sampling ◽  
Transition Path ◽  
Transition Path Sampling ◽  
Safety And Reliability

scholarly journals Inverse enzyme isotope effects in human purine nucleoside phosphorylase with heavy asparagine labels

2018 ◽  
Vol 115 (27) ◽  
pp. E6209-E6216 ◽  
Author(s):  
Rajesh K. Harijan ◽  
Ioanna Zoi ◽  
Dimitri Antoniou ◽  
Steven D. Schwartz ◽  
Vern L. Schramm
Keyword(s):  
Transition State ◽  
Purine Nucleoside Phosphorylase ◽  
Isotope Effects ◽  
Catalytic Site ◽  
Path Sampling ◽  
Transition Path ◽  
Transition Path Sampling ◽  
Steady State Kinetics ◽  
Leaving Group ◽  
Transition State Barrier

Transition path-sampling calculations with several enzymes have indicated that local catalytic site femtosecond motions are linked to transition state barrier crossing. Experimentally, femtosecond motions can be perturbed by labeling the protein with amino acids containing 13C, 15N, and nonexchangeable 2H. A slowed chemical step at the catalytic site with variable effects on steady-state kinetics is usually observed for heavy enzymes. Heavy human purine nucleoside phosphorylase (PNP) is slowed significantly (kchemlight/kchemheavy = 1.36). An asparagine (Asn243) at the catalytic site is involved in purine leaving-group activation in the PNP catalytic mechanism. In a PNP produced with isotopically heavy asparagines, the chemical step is faster (kchemlight/kchemheavy = 0.78). When all amino acids in PNP are heavy except for the asparagines, the chemical step is also faster (kchemlight/kchemheavy = 0.71). Substrate-trapping experiments provided independent confirmation of improved catalysis in these constructs. Transition path-sampling analysis of these partially labeled PNPs indicate altered femtosecond catalytic site motions with improved Asn243 interactions to the purine leaving group. Altered transition state barrier recrossing has been proposed as an explanation for heavy-PNP isotope effects but is incompatible with these isotope effects. Rate-limiting product release governs steady-state kinetics in this enzyme, and kinetic constants were unaffected in the labeled PNPs. The study suggests that mass-constrained femtosecond motions at the catalytic site of PNP can improve transition state barrier crossing by more frequent sampling of essential catalytic site contacts.

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