Cited by 173Protein Structure and DynamicsAdvanced Physical and Chemical Molecular InteractionsMarkov Chains and Monte Carlo Methods

Projected and hidden Markov models for calculating kinetics and metastable states of complex molecules

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Noé, Frank, Wu, Hao, Prinz, Jan-Hendrik, Plattner, Nuria·2013·The Journal of Chemical Physics

Abstract

Markov state models (MSMs) have been successful in computing metastable states, slow relaxation timescales and associated structural changes, and stationary or kinetic experimental observables of complex molecules from large amounts of molecular dynamics simulation data. However, MSMs approximate the true dynamics by assuming a Markov chain on a clusters discretization of the state space. This approximation is difficult to make for high-dimensional biomolecular systems, and the quality and reproducibility of MSMs has, therefore, been limited. Here, we discard the assumption that dynamics are Markovian on the discrete clusters. Instead, we only assume that the full phase-space molecular dynamics is Markovian, and a projection of this full dynamics is observed on the discrete states, leading to the concept of Projected Markov Models (PMMs). Robust estimation methods for PMMs are not yet available, but we derive a practically feasible approximation via Hidden Markov Models (HMMs). It is shown how various molecular observables of interest that are often computed from MSMs can be computed from HMMs/PMMs. The new framework is applicable to both, simulation and single-molecule experimental data. We demonstrate its versatility by applications to educative model systems, a 1 ms Anton MD simulation of the bovine pancreatic trypsin inhibitor protein, and an optical tweezer force probe trajectory of an RNA hairpin.

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  • PMMs can be efficiently estimated by Hidden Markov model techniques, and the resulting HMM is as easy to interpret as an MSM.

    “It was shown that PMMs can be efficiently estimated by Hidden Markov model techniques (HMMs), and that the resulting HMM is as easy to interpret as an MSM.”

    From Markov state models of biomolecular conformational dynamics (2014) · cites this paper as [3]

    Section VI (Conclusions; page unavailable) says that, under specified metastability and timescale-separation conditions, PMMs can be approximated by HMMs that can be efficiently estimated. It also says HMM-derived observables can be readily interpreted, but does not establish that an HMM is as easy to interpret as an MSM. The citing sentence omits the conditions on the approximation. (LLM, conf=0.85)

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Authors
Noé, F., Wu, H., Prinz, J.-H., & Plattner, N.
Affiliations
Freie Universität Berlin (DE)
Venue
The Journal of Chemical Physics
Published
2013-11-13
Volume
139
Issue
18
Pages
184114-184114
ISSN
  • 0021-9606 (ISSN-L)
  • 1089-7690
OpenAlex
W2077760098
Cited by
173
References
48
Citations by year
2026: 10 · 2025: 16 · 2024: 9 · 2023: 10 · 2022: 18 · 2021: 18 · 2020: 11 · 2019: 16 · 2018: 22 · 2017: 13 · 2016: 12 · 2015: 12 · 2014: 6
FWCI
4.45
Type
journal article
Language
en
Open access
Locations
  • The Journal of Chemical Physics (publishedVersion)
  • PubMed (publishedVersion)
  • arXiv (Cornell University) (submittedVersion)
  • Refubium (Universitätsbibliothek der Freien Universität Berlin) (submittedVersion)
  • arXiv (Cornell University)
Funders
  • European Commission (SFB 958)
  • Deutsche Forschungsgemeinschaft (825/2, SFB 958)
  • Einstein Stiftung Berlin
  • Freie Universität Berlin
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Physical Sciences › Chemistry › Physical and Theoretical Chemistry › Advanced Physical and Chemical Molecular Interactions
  • Physical Sciences › Mathematics › Statistics and Probability › Markov Chains and Monte Carlo Methods
Keywords
hidden Markov models, Markov state models, metastable states, slow relaxation, non-Markovian dynamics, biomolecular dynamics, single-molecule force spectroscopy, optical tweezers, RNA hairpin, aprotinin, conformational kinetics
MeSH terms
Animals, Cattle, Aprotinin, Kinetics, RNA, Molecular Dynamics Simulation

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