Measuring physical quantities in the nanometric region inside single cells is of great importance for understanding cellular activity. Thus, the development of biocompatible, sensitive, and reliable nanobiosensors is essential for progress in biological research. Diamond nanoparticles containing nitrogen-vacancy centers (NVCs), referred to as fluorescent nanodiamonds (FNDs), have recently emerged as the sensors that show great promise for ultrasensitive nanosensing of physical quantities. FNDs emit stable fluorescence without photobleaching. Additionally, their distinctive magneto-optical properties enable an optical readout of the quantum states of the electron spin in NVC under ambient conditions. These properties enable the quantitative sensing of physical parameters (temperature, magnetic field, electric field, pH, etc.) in the vicinity of an FND; hence, FNDs are often described as "quantum sensors". In this review, recent advancements in biosensing applications of FNDs are summarized. First, the principles of orientation and temperature sensing using FND quantum sensors are explained. Next, we introduce surface coating techniques indispensable for controlling the physicochemical properties of FNDs. The achievements of practical biological sensing using surface-coated FNDs, including orientation, temperature, and thermal conductivity, are then highlighted. Finally, the advantages, challenges, and perspectives of the quantum sensing of FND are discussed. This review article is an extended version of the Japanese article, In Situ Measurement of Intracellular Thermal Conductivity Using Diamond Nanoparticle, published in SEIBUTSU BUTSURI Vol. 62, p. 122-124 (2022).
测量单细胞内纳米区域的物理量对于了解细胞活动具有重要意义。因此,开发具有生物相容性、敏感性和可靠性的纳米生物传感器对生物研究的进步至关重要。含有氮空位中心(nvc)的纳米金刚石被称为荧光纳米金刚石(FNDs),近年来作为一种传感器出现,在物理量的超灵敏纳米传感方面显示出巨大的前景。fnd发出稳定的荧光,不发生光漂白。此外,它们独特的磁光特性使其能够在环境条件下光学读出NVC中电子自旋的量子态。这些特性使FND附近的物理参数(温度、磁场、电场、pH等)的定量传感成为可能;因此,fnd通常被描述为“量子传感器”。本文综述了近年来FNDs在生物传感领域的研究进展。首先,阐述了FND量子传感器的取向和温度传感原理。其次,我们介绍了控制fnd的物理化学性质必不可少的表面涂层技术。然后强调了使用表面涂层fnd的实际生物传感的成就,包括取向,温度和导热性。最后,讨论了FND量子传感的优势、挑战和前景。这篇综述文章是日本文章《使用金刚石纳米颗粒原位测量细胞内热导率》的扩展版,发表在SEIBUTSU BUTSURI Vol. 62, p. 122-124(2022)。
{"title":"Quantum nanodiamonds for sensing of biological quantities: Angle, temperature, and thermal conductivity.","authors":"Shingo Sotoma, Hirotaka Okita, Shunsuke Chuma, Yoshie Harada","doi":"10.2142/biophysico.bppb-v19.0034","DOIUrl":"https://doi.org/10.2142/biophysico.bppb-v19.0034","url":null,"abstract":"<p><p>Measuring physical quantities in the nanometric region inside single cells is of great importance for understanding cellular activity. Thus, the development of biocompatible, sensitive, and reliable nanobiosensors is essential for progress in biological research. Diamond nanoparticles containing nitrogen-vacancy centers (NVCs), referred to as fluorescent nanodiamonds (FNDs), have recently emerged as the sensors that show great promise for ultrasensitive nanosensing of physical quantities. FNDs emit stable fluorescence without photobleaching. Additionally, their distinctive magneto-optical properties enable an optical readout of the quantum states of the electron spin in NVC under ambient conditions. These properties enable the quantitative sensing of physical parameters (temperature, magnetic field, electric field, pH, etc.) in the vicinity of an FND; hence, FNDs are often described as \"quantum sensors\". In this review, recent advancements in biosensing applications of FNDs are summarized. First, the principles of orientation and temperature sensing using FND quantum sensors are explained. Next, we introduce surface coating techniques indispensable for controlling the physicochemical properties of FNDs. The achievements of practical biological sensing using surface-coated FNDs, including orientation, temperature, and thermal conductivity, are then highlighted. Finally, the advantages, challenges, and perspectives of the quantum sensing of FND are discussed. This review article is an extended version of the Japanese article, In Situ Measurement of Intracellular Thermal Conductivity Using Diamond Nanoparticle, published in SEIBUTSU BUTSURI Vol. 62, p. 122-124 (2022).</p>","PeriodicalId":8976,"journal":{"name":"Biophysics and Physicobiology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-09-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/9c/b4/19_e190034.PMC9592573.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40452694","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2022-08-30eCollection Date: 2022-01-01DOI: 10.2142/biophysico.bppb-v19.0033
Kayo Hibino
The Biophysical Societies of Japan and the Indian Biophysical Society regularly organize India-Japan joint symposiums and other exchange opportunities for further development of the biophysics field and international exchange of scientists. Here I report on the 44th Indian Biophysical Society Meeting [1] held in Mumbai, India as a hybrid of the online meeting, on March 30-31 and April 1, 2022. The conference theme was "Conceptual Advances in Biophysics and its Applications", and over 300 scientists and students from all over the world participated. The conference hosted five lectures, including the GN Ramachandran Lecture, and 24 invited talks in seven sessions on: 1) Protein-Protein Interactions, 2) Protein Folding, 3) Aggregation & Related Diseases, 4) Molecular & Cellular Biophysics, 5) Structural Biology & its applications, 6) Protein Conformational Dynamics, and 7) Biophysical Techniques & Disease Intervention. It also had
{"title":"Participation in 44th Indian Biophysical Society Meeting.","authors":"Kayo Hibino","doi":"10.2142/biophysico.bppb-v19.0033","DOIUrl":"https://doi.org/10.2142/biophysico.bppb-v19.0033","url":null,"abstract":"The Biophysical Societies of Japan and the Indian Biophysical Society regularly organize India-Japan joint symposiums and other exchange opportunities for further development of the biophysics field and international exchange of scientists. Here I report on the 44th Indian Biophysical Society Meeting [1] held in Mumbai, India as a hybrid of the online meeting, on March 30-31 and April 1, 2022. The conference theme was \"Conceptual Advances in Biophysics and its Applications\", and over 300 scientists and students from all over the world participated. The conference hosted five lectures, including the GN Ramachandran Lecture, and 24 invited talks in seven sessions on: 1) Protein-Protein Interactions, 2) Protein Folding, 3) Aggregation & Related Diseases, 4) Molecular & Cellular Biophysics, 5) Structural Biology & its applications, 6) Protein Conformational Dynamics, and 7) Biophysical Techniques & Disease Intervention. It also had","PeriodicalId":8976,"journal":{"name":"Biophysics and Physicobiology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-08-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/ac/92/19_e190033.PMC9592566.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40452695","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2022-08-30eCollection Date: 2022-01-01DOI: 10.2142/biophysico.bppb-v19.0032
Ryo Iizuka, Hirohito Yamazaki, Sotaro Uemura
Single-molecule technologies can provide detailed information regarding molecular mechanisms and interactions that cannot easily be studied on the bulk scale; generally, individual molecular behaviors cannot be distinguished, and only average characteristics can be measured. Nevertheless, the development of the single-molecule sequencer had a significant impact on conventional in vitro single-molecule research, featuring automated equipment, high-throughput chips, and automated analysis systems. However, the utilization of sequencing technology in in vitro single-molecule research is not yet globally prevalent, owing to the large gap between highly organized single-molecule sequencing and manual-based in vitro single-molecule research. Here, we describe the principles of zero-mode waveguides (ZMWs) and nanopore methods used as single-molecule DNA sequencing techniques, and provide examples of functional biological measurements beyond DNA sequencing that contribute to a global understanding of the current applications of these sequencing technologies. Furthermore, through a comparison of these two technologies, we discuss future applications of DNA sequencing technologies in in vitro single-molecule research.
{"title":"Zero-mode waveguides and nanopore-based sequencing technologies accelerate single-molecule studies.","authors":"Ryo Iizuka, Hirohito Yamazaki, Sotaro Uemura","doi":"10.2142/biophysico.bppb-v19.0032","DOIUrl":"https://doi.org/10.2142/biophysico.bppb-v19.0032","url":null,"abstract":"<p><p>Single-molecule technologies can provide detailed information regarding molecular mechanisms and interactions that cannot easily be studied on the bulk scale; generally, individual molecular behaviors cannot be distinguished, and only average characteristics can be measured. Nevertheless, the development of the single-molecule sequencer had a significant impact on conventional <i>in vitro</i> single-molecule research, featuring automated equipment, high-throughput chips, and automated analysis systems. However, the utilization of sequencing technology in <i>in vitro</i> single-molecule research is not yet globally prevalent, owing to the large gap between highly organized single-molecule sequencing and manual-based <i>in vitro</i> single-molecule research. Here, we describe the principles of zero-mode waveguides (ZMWs) and nanopore methods used as single-molecule DNA sequencing techniques, and provide examples of functional biological measurements beyond DNA sequencing that contribute to a global understanding of the current applications of these sequencing technologies. Furthermore, through a comparison of these two technologies, we discuss future applications of DNA sequencing technologies in <i>in vitro</i> single-molecule research.</p>","PeriodicalId":8976,"journal":{"name":"Biophysics and Physicobiology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-08-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/61/cb/19_e190032.PMC9592571.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40452699","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2022-08-27eCollection Date: 2022-01-01DOI: 10.2142/biophysico.bppb-v19.0029
Madoka Suzuki, Kotaro Oyama
Muscles are the source of mechanical force. Muscles enable us to move our arms and legs, speak, pump blood, and digest food. Muscle mechanics has been an important subject in biophysics. Accordingly, it is now possible to explain how mechanical force is produced and assembled at all levels of the hierarchy of the muscle contractile system, that is, from a single protein molecule at the smallest scale, to an assembly of the molecules (sarcomere; a highly ordered bipolar structure mainly composed of actin filaments that are protein polymers of actin monomers, and their counterpart myosin filaments that are of myosin motor proteins), to a myofibril (assembly of sarcomeres connected in series) and muscle cell, and finally, to a tissue. Then, are there no intriguing questions that can be asked regarding biophysics? We have organized a symposium titled “The Future of Muscle is Now” at the 60th Annual Meeting of the Biophysical Society of Japan, held in September 2022 (Figure 1). In the symposium, we intend to demonstrate that the previously mentioned tragic perspective may be incorrect.
{"title":"A five-course meal symposium on \"The Future of Muscle is Now\".","authors":"Madoka Suzuki, Kotaro Oyama","doi":"10.2142/biophysico.bppb-v19.0029","DOIUrl":"https://doi.org/10.2142/biophysico.bppb-v19.0029","url":null,"abstract":"Muscles are the source of mechanical force. Muscles enable us to move our arms and legs, speak, pump blood, and digest food. Muscle mechanics has been an important subject in biophysics. Accordingly, it is now possible to explain how mechanical force is produced and assembled at all levels of the hierarchy of the muscle contractile system, that is, from a single protein molecule at the smallest scale, to an assembly of the molecules (sarcomere; a highly ordered bipolar structure mainly composed of actin filaments that are protein polymers of actin monomers, and their counterpart myosin filaments that are of myosin motor proteins), to a myofibril (assembly of sarcomeres connected in series) and muscle cell, and finally, to a tissue. Then, are there no intriguing questions that can be asked regarding biophysics? We have organized a symposium titled “The Future of Muscle is Now” at the 60th Annual Meeting of the Biophysical Society of Japan, held in September 2022 (Figure 1). In the symposium, we intend to demonstrate that the previously mentioned tragic perspective may be incorrect.","PeriodicalId":8976,"journal":{"name":"Biophysics and Physicobiology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-08-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/45/43/19_e190029.PMC9592567.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40462102","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2022-08-27eCollection Date: 2022-01-01DOI: 10.2142/biophysico.bppb-v19.0031
Makito Miyazaki, Takahiro Kosugi
{"title":"Uncovering the design principles of supramolecular assemblies through manipulation of the structures, dynamics, and functions.","authors":"Makito Miyazaki, Takahiro Kosugi","doi":"10.2142/biophysico.bppb-v19.0031","DOIUrl":"10.2142/biophysico.bppb-v19.0031","url":null,"abstract":"","PeriodicalId":8976,"journal":{"name":"Biophysics and Physicobiology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-08-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/7c/5d/19_e190031.PMC9592565.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40452700","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2022-08-27eCollection Date: 2022-01-01DOI: 10.2142/biophysico.bppb-v19.0030
Kumiko Hayashi, Jakia Jannat Keya
{"title":"Japan-US symposium on motor proteins and associated single-molecule biophysics.","authors":"Kumiko Hayashi, Jakia Jannat Keya","doi":"10.2142/biophysico.bppb-v19.0030","DOIUrl":"10.2142/biophysico.bppb-v19.0030","url":null,"abstract":"","PeriodicalId":8976,"journal":{"name":"Biophysics and Physicobiology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-08-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/b2/0e/19_e190030.PMC9592572.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40452698","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2022-08-24eCollection Date: 2022-01-01DOI: 10.2142/biophysico.bppb-v19.0028
Ryo Kitahara, Tomoshi Kameda
In recent years, various intracellular components, such as P-bodies, nucleoli, and stress granules, have been shown to be aggregates of proteins and RNA via liquid–liquid phase separation (LLPS) [1]. Since such protein granules can reversibly form, disappear, and play their respective roles in the cell, they are called membraneless organelles. To date, many proteins, especially nuclear proteins, and artificial peptides have been reported to form protein granules, namely condensed liquid droplets, via LLPS (Figure 1) [2,3]. Interestingly, amyloid fibril formation is gradually accelerated in droplets [4]. By elucidating the formation mechanism of irreversible aggregates from the homogeneous phase state (1-phase) of proteins via liquid droplets in vitro and in vivo, effective drugs can be developed for neurodegenerative diseases. To discuss the cutting-edge research on the LLPS of biopolymers [5-9], the “Phase Separation by Biopolymers: Basics and Applications” symposium will be held at the 60th Annual Meeting of the Biophysical Society of Japan in September, 2022. The invited speakers at the symposium will be Ryo Kitahara, Akira Nomoto, Shinji Kajimoto, Kiyoto Kamagata, and Tomoshi Kameda. Kitahara et al. will introduce a pressure-temperature phase diagram of LLPS for fused in sarcoma (FUS) and the application of a pressure-jump spectroscopic technique to study the formation and vanishing dynamics of FUS-LLPS [6,7]. Nomoto et al. will discuss the solubility parameters of amino acids during LLPS and the aggregation of proteins, based on the solubility of aromatic amino acids in a solution containing 20 different amino acids [5]. Kajimoto et al. will explain Raman and Brillouin microscopy as a tool for quantitative analysis of LLPS. This method is a powerful technique to determine the chemical nature of LLPS and its relationship with protein aggregation [9]. Kamagara et al. will introduce rational peptide design for regulating LLPS on the basis of residue-residue contact energy. The effects of designed peptides on p53 LLPS analysis will be discussed [8]. Kameda et al. will introduce theoretical approaches combined with molecular dynamics simulations and machine learning. The aggregation nature of tetra-peptides will be discussed.
{"title":"Phase separation by biopolymers: Basics and applications.","authors":"Ryo Kitahara, Tomoshi Kameda","doi":"10.2142/biophysico.bppb-v19.0028","DOIUrl":"https://doi.org/10.2142/biophysico.bppb-v19.0028","url":null,"abstract":"In recent years, various intracellular components, such as P-bodies, nucleoli, and stress granules, have been shown to be aggregates of proteins and RNA via liquid–liquid phase separation (LLPS) [1]. Since such protein granules can reversibly form, disappear, and play their respective roles in the cell, they are called membraneless organelles. To date, many proteins, especially nuclear proteins, and artificial peptides have been reported to form protein granules, namely condensed liquid droplets, via LLPS (Figure 1) [2,3]. Interestingly, amyloid fibril formation is gradually accelerated in droplets [4]. By elucidating the formation mechanism of irreversible aggregates from the homogeneous phase state (1-phase) of proteins via liquid droplets in vitro and in vivo, effective drugs can be developed for neurodegenerative diseases. To discuss the cutting-edge research on the LLPS of biopolymers [5-9], the “Phase Separation by Biopolymers: Basics and Applications” symposium will be held at the 60th Annual Meeting of the Biophysical Society of Japan in September, 2022. The invited speakers at the symposium will be Ryo Kitahara, Akira Nomoto, Shinji Kajimoto, Kiyoto Kamagata, and Tomoshi Kameda. Kitahara et al. will introduce a pressure-temperature phase diagram of LLPS for fused in sarcoma (FUS) and the application of a pressure-jump spectroscopic technique to study the formation and vanishing dynamics of FUS-LLPS [6,7]. Nomoto et al. will discuss the solubility parameters of amino acids during LLPS and the aggregation of proteins, based on the solubility of aromatic amino acids in a solution containing 20 different amino acids [5]. Kajimoto et al. will explain Raman and Brillouin microscopy as a tool for quantitative analysis of LLPS. This method is a powerful technique to determine the chemical nature of LLPS and its relationship with protein aggregation [9]. Kamagara et al. will introduce rational peptide design for regulating LLPS on the basis of residue-residue contact energy. The effects of designed peptides on p53 LLPS analysis will be discussed [8]. Kameda et al. will introduce theoretical approaches combined with molecular dynamics simulations and machine learning. The aggregation nature of tetra-peptides will be discussed.","PeriodicalId":8976,"journal":{"name":"Biophysics and Physicobiology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-08-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/1b/8e/19_e190028.PMC9592568.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40462101","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2022-08-23eCollection Date: 2021-01-01DOI: 10.2142/biophysico.bppb-v18.s005
In the previous chapter, the rule was that if a person with 0 gaming chips was hit, the number of trials were incremented without debt. An interesting variation of this rule involves elimination of the player via inclusion of the concept of bankruptcy from society, i.e., a person with 0 gaming chips is eliminated from the game (Fig. 3.1)3.1. In this case, since the total number of gaming chips will be the same, however, the number of players will decrease, therefore the average number of gaming chips per person will increase. Nevertheless, the number of bankruptcies (persons with 0 gaming chips) will continue to increase, as such persons appear every moment (Fig. 3.1; Bar at the left end of the figure on the right). If we keep it going, only a small number of rich people will survive.
{"title":"Chapter 3: Changing the Rules.","authors":"","doi":"10.2142/biophysico.bppb-v18.s005","DOIUrl":"https://doi.org/10.2142/biophysico.bppb-v18.s005","url":null,"abstract":"In the previous chapter, the rule was that if a person with 0 gaming chips was hit, the number of trials were incremented without debt. An interesting variation of this rule involves elimination of the player via inclusion of the concept of bankruptcy from society, i.e., a person with 0 gaming chips is eliminated from the game (Fig. 3.1)3.1. In this case, since the total number of gaming chips will be the same, however, the number of players will decrease, therefore the average number of gaming chips per person will increase. Nevertheless, the number of bankruptcies (persons with 0 gaming chips) will continue to increase, as such persons appear every moment (Fig. 3.1; Bar at the left end of the figure on the right). If we keep it going, only a small number of rich people will survive.","PeriodicalId":8976,"journal":{"name":"Biophysics and Physicobiology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-08-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/de/65/18_S025.PMC9465403.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33484764","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2022-08-23eCollection Date: 2022-01-01DOI: 10.2142/biophysico.bppb-v19.0027
Takeru Kameda, Akinori Awazu, Yuichi Togashi
With the recent progress in structural biology and genome biology, structural dynamics of molecular systems that include nucleic acids has attracted attention in the context of gene regulation. The structure-function relationship is an important topic that highlights the importance of the physicochemical properties of nucleotides, as well as that of amino acids in proteins. Simulations are a useful tool for the detailed analysis of molecular dynamics that complement experiments in molecular biology; however, molecular simulation of nucleic acids is less well developed than that of proteins partly due to the physical nature of nucleic acids. In this review, we briefly describe the current status and future directions of the field as a guide to promote collaboration between experimentalists and computational biologists.
{"title":"Molecular dynamics analysis of biomolecular systems including nucleic acids.","authors":"Takeru Kameda, Akinori Awazu, Yuichi Togashi","doi":"10.2142/biophysico.bppb-v19.0027","DOIUrl":"https://doi.org/10.2142/biophysico.bppb-v19.0027","url":null,"abstract":"<p><p>With the recent progress in structural biology and genome biology, structural dynamics of molecular systems that include nucleic acids has attracted attention in the context of gene regulation. The structure-function relationship is an important topic that highlights the importance of the physicochemical properties of nucleotides, as well as that of amino acids in proteins. Simulations are a useful tool for the detailed analysis of molecular dynamics that complement experiments in molecular biology; however, molecular simulation of nucleic acids is less well developed than that of proteins partly due to the physical nature of nucleic acids. In this review, we briefly describe the current status and future directions of the field as a guide to promote collaboration between experimentalists and computational biologists.</p>","PeriodicalId":8976,"journal":{"name":"Biophysics and Physicobiology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-08-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/17/65/19_e190027.PMC9592887.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40452692","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Ciliates are swimming microorganisms in aquatic environments. Habitats where ciliates accumulate include nutrient-rich solid-liquid interfaces such as pond bottom walls and waterweed surfaces. The ciliates stay near the walls to survive. We investigated the dynamics of the near-wall behavior of ciliates. In experiments, the ciliates were made to slide on a flat wall of glass substrate. When encountering the wall, the wall-side cilia of the cells stop their motion and lose their propelling activity, which indicates that the ciliates have a mechano-sensing system for cilia beating. Based on the experimental results, we hypothesized that the ciliary thrust force that propels the cell body becomes asymmetric, and the asymmetry of the thrust force generates a head-down torque to keep the cell sliding on the wall. To prove this hypothesis, we performed numerical simulations by using a developed hydrodynamic model for swimming ciliates. The model revealed that the loss of cilia activity on the wall side physically induces a sliding motion, and the aspect ratio of the cell body and effective cilium area are critical functions for the sliding behavior on a wall. In addition, we investigated the stability of the sliding motion against an external flow. We found that ciliates slide upstream on a wall. Interestingly, the dynamics of this upstream sliding, called rheotaxis, were also explained by the identical physical conditions for no-flow sliding. Only two simple physical conditions are required to explain the dynamics of ciliate survival behavior. This review article is an extended version of the Japanese article, Fluid Dynamic Model Reveals a Mechano-sensing System Underlying the Behavior of Ciliates, published in SEIBUTSU BUTSURI Vol. 61, p. 16-19 (2021).
纤毛虫是水生环境中的游动微生物。纤毛虫聚集的栖息地包括营养丰富的固液界面,如池塘底壁和水草表面。纤毛虫在墙壁附近生存。我们研究了纤毛虫近壁行为的动力学。在实验中,纤毛虫在玻璃基底的平壁上滑动。当细胞的壁侧纤毛遇到壁面时,细胞的壁侧纤毛停止运动,失去推进活动,这表明纤毛具有对纤毛跳动的机械感应系统。根据实验结果,我们假设推动细胞体的纤毛推力变得不对称,而推力的不对称产生了一个头部向下的扭矩来保持细胞在壁上滑动。为了证明这一假设,我们使用已开发的游泳纤毛虫水动力学模型进行了数值模拟。该模型表明,细胞壁纤毛活性的丧失在物理上引起了细胞壁的滑动运动,而细胞体长径比和有效纤毛面积是细胞壁滑动行为的关键函数。此外,我们研究了滑动运动对外部流动的稳定性。我们发现纤毛虫沿着墙壁向上游滑动。有趣的是,这种上游滑动的动力学称为流变性,也可以用无流滑动的相同物理条件来解释。只需要两个简单的物理条件就可以解释纤毛虫生存行为的动力学。这篇综述文章是日本文章《流体动力学模型揭示了纤毛虫行为背后的机械传感系统》的扩展版,发表于SEIBUTSU BUTSURI Vol. 61, p. 16-19(2021)。
{"title":"Simple dynamics underlying the survival behaviors of ciliates.","authors":"Takuya Ohmura, Yukinori Nishigami, Masatoshi Ichikawa","doi":"10.2142/biophysico.bppb-v19.0026","DOIUrl":"https://doi.org/10.2142/biophysico.bppb-v19.0026","url":null,"abstract":"<p><p>Ciliates are swimming microorganisms in aquatic environments. Habitats where ciliates accumulate include nutrient-rich solid-liquid interfaces such as pond bottom walls and waterweed surfaces. The ciliates stay near the walls to survive. We investigated the dynamics of the near-wall behavior of ciliates. In experiments, the ciliates were made to slide on a flat wall of glass substrate. When encountering the wall, the wall-side cilia of the cells stop their motion and lose their propelling activity, which indicates that the ciliates have a mechano-sensing system for cilia beating. Based on the experimental results, we hypothesized that the ciliary thrust force that propels the cell body becomes asymmetric, and the asymmetry of the thrust force generates a head-down torque to keep the cell sliding on the wall. To prove this hypothesis, we performed numerical simulations by using a developed hydrodynamic model for swimming ciliates. The model revealed that the loss of cilia activity on the wall side physically induces a sliding motion, and the aspect ratio of the cell body and effective cilium area are critical functions for the sliding behavior on a wall. In addition, we investigated the stability of the sliding motion against an external flow. We found that ciliates slide upstream on a wall. Interestingly, the dynamics of this upstream sliding, called rheotaxis, were also explained by the identical physical conditions for no-flow sliding. Only two simple physical conditions are required to explain the dynamics of ciliate survival behavior. This review article is an extended version of the Japanese article, Fluid Dynamic Model Reveals a Mechano-sensing System Underlying the Behavior of Ciliates, published in SEIBUTSU BUTSURI Vol. 61, p. 16-19 (2021).</p>","PeriodicalId":8976,"journal":{"name":"Biophysics and Physicobiology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"2022-08-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/07/96/19_e190026.PMC9465405.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33484499","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}