Evidence map›Paper›PMID 36580448›Full record

ArticlePLoS computational biology2022

Development of hidden Markov modeling method for molecular orientations and structure estimation from high-speed atomic force microscopy time-series images.

Tomonori Ogane, Daisuke Noshiro, Toshio Ando, Atsuko Yamashita, Yuji Sugita, Yasuhiro Matsunaga

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Article in PLoS computational biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

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4citing papers in PubMed
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3 · Its place in the literature

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4 citing papers in PubMed.

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5 · Who and what money

Authors and funding

6 authors.

Tomonori OganeGraduate School of Science and Engineering, Saitama University, Saitama, Japan.
Daisuke NoshiroNano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kanazawa, Japan.ORCID 0000-0001-7024-2054
Toshio AndoNano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kanazawa, Japan.
Atsuko YamashitaGraduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University, Okayama, Japan.
Yuji SugitaComputational Biophysics Research Team, RIKEN Center for Computational Science, Kobe, Japan.
Yasuhiro MatsunagaGraduate School of Science and Engineering, Saitama University, Saitama, Japan.ORCID 0000-0003-2872-3908

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

High-speed atomic force microscopy (HS-AFM) is a powerful technique for capturing the time-resolved behavior of biomolecules. However, structural information in HS-AFM images is limited to the surface geometry of a sample molecule. Inferring latent three-dimensional structures from the surface geometry is thus important for getting more insights into conformational dynamics of a target biomolecule. Existing methods for estimating the structures are based on the rigid-body fitting of candidate structures to each frame of HS-AFM images. Here, we extend the existing frame-by-frame rigid-body fitting analysis to multiple frames to exploit orientational correlations of a sample molecule between adjacent frames in HS-AFM data due to the interaction with the stage. In the method, we treat HS-AFM data as time-series data, and they are analyzed with the hidden Markov modeling. Using simulated HS-AFM images of the taste receptor type 1 as a test case, the proposed method shows a more robust estimation of molecular orientations than the frame-by-frame analysis. The method is applicable in integrative modeling of conformational dynamics using HS-AFM data.

Indexed as

Microscopy, Atomic ForceMarkov ChainsReceptors, G-Protein-CoupledReceptors, G-Protein-Coupledtaste receptors, type 1

Identifiers

PMID36580448
PMCPMC9833559

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.