Biophysical reviewsPub Date : 2023-08-29eCollection Date: 2023-10-01DOI: 10.1007/s12551-023-01116-y
D V Vetoshkina, M M Borisova-Mubarakshina
{"title":"Reversible protein phosphorylation in higher plants: focus on state transitions.","authors":"D V Vetoshkina, M M Borisova-Mubarakshina","doi":"10.1007/s12551-023-01116-y","DOIUrl":"10.1007/s12551-023-01116-y","url":null,"abstract":"<p><p>Reversible protein phosphorylation is one of the comprehensive mechanisms of cell metabolism regulation in eukaryotic organisms. The review describes the impact of the reversible protein phosphorylation on the regulation of growth and development as well as in adaptation pathways and signaling network in higher plant cells. The main part of the review is devoted to the role of the reversible phosphorylation of light-harvesting proteins of photosystem II and the state transition process in fine-tuning the photosynthetic activity of chloroplasts. A separate section of the review is dedicated to comparing the mechanisms and functional significance of state transitions in higher plants, algae, and cyanobacteria that allows the evolution aspects of state transitions meaning in various organisms to be discussed. Environmental factors affecting the state transitions are also considered. Additionally, we gain insight into the possible influence of STN7-dependent phosphorylation of the target proteins on the global network of reversible protein phosphorylation in plant cells as well as into the probable effect of the STN7 kinase inhibition on long-term acclimation pathways in higher plants.</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":null,"pages":null},"PeriodicalIF":4.9,"publicationDate":"2023-08-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10643769/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"48576734","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}
Biophysical reviewsPub Date : 2023-08-29eCollection Date: 2023-12-01DOI: 10.1007/s12551-023-01112-2
Fria Hossein, Panagiota Angeli
{"title":"A review of acoustofluidic separation of bioparticles.","authors":"Fria Hossein, Panagiota Angeli","doi":"10.1007/s12551-023-01112-2","DOIUrl":"10.1007/s12551-023-01112-2","url":null,"abstract":"<p><p>Acoustofluidics is an emerging interdisciplinary research field that involves the integration of acoustics and microfluidics to address challenges in various scientific areas. This technology has proven to be a powerful tool for separating biological targets from complex fluids due to its label-free, biocompatible, and contact-free nature. Considering a careful designing process and tuning the acoustic field particles can be separated with high yield. Recently the advancement of acoustofluidics led to the development of point-of-care devices for separations of micro particles which address many of the limitations of conventional separation tools. This review article discusses the working principles and different approaches of acoustofluidic separation and provides a synopsis of its traditional and emerging applications, including the theory and mechanism of acoustofluidic separation, blood component separation, cell washing, fluorescence-activated cell sorting, circulating tumor cell isolation, and exosome isolation. The technology offers great potential for solving clinical problems and advancing scientific research.</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":null,"pages":null},"PeriodicalIF":4.9,"publicationDate":"2023-08-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10771489/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"43424441","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}
Biophysical reviewsPub Date : 2023-08-26eCollection Date: 2023-10-01DOI: 10.1007/s12551-023-01111-3
Evgeniy V Dubrovin
{"title":"<b>Atomic force microscopy-based approaches for single-molecule investigation of nucleic acid</b>-<b>protein complexes</b>.","authors":"Evgeniy V Dubrovin","doi":"10.1007/s12551-023-01111-3","DOIUrl":"10.1007/s12551-023-01111-3","url":null,"abstract":"<p><p>The interaction of nucleic acids with proteins plays an important role in many fundamental biological processes in living cells, including replication, transcription, and translation. Therefore, understanding nucleic acid-protein interaction is of high relevance in many areas of biology, medicine and technology. During almost four decades of its existence atomic force microscopy (AFM) accumulated a significant experience in investigation of biological molecules at a single-molecule level. AFM has become a powerful tool of molecular biology and biophysics providing unique information about properties, structure, and functioning of biomolecules. Despite a great variety of nucleic acid-protein systems under AFM investigations, there are a number of typical approaches for such studies. This review is devoted to the analysis of the typical AFM-based approaches of investigation of DNA (RNA)-protein complexes with a major focus on transcription studies. The basic strategies of AFM analysis of nucleic acid-protein complexes including investigation of the products of DNA-protein reactions and real-time dynamics of DNA-protein interaction are categorized and described by the example of the most relevant research studies. The described approaches and protocols have many universal features and, therefore, are applicable for future AFM studies of various nucleic acid-protein systems.</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":null,"pages":null},"PeriodicalIF":4.9,"publicationDate":"2023-08-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10643717/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"45521479","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}
Biophysical reviewsPub Date : 2023-08-26eCollection Date: 2023-12-01DOI: 10.1007/s12551-023-01118-w
Wilma K Olson, John H Maddocks, Pablo D Dans, Thomas H Cheatham, Sarah Harris, Charlie Laughton, Modesto Orozco, Lois Pollack
{"title":"An open call for contributions to a special issue of <i>Biophysical Reviews</i> focused on multiscale simulations of DNA from electrons to nucleosomes.","authors":"Wilma K Olson, John H Maddocks, Pablo D Dans, Thomas H Cheatham, Sarah Harris, Charlie Laughton, Modesto Orozco, Lois Pollack","doi":"10.1007/s12551-023-01118-w","DOIUrl":"10.1007/s12551-023-01118-w","url":null,"abstract":"","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":null,"pages":null},"PeriodicalIF":4.9,"publicationDate":"2023-08-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10771543/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"44879581","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}
Biophysical reviewsPub Date : 2023-08-25eCollection Date: 2023-08-01DOI: 10.1007/s12551-023-01114-0
Silvia Del V Alonso, F Luis González Flecha
{"title":"Fifty years of biophysics in Argentina.","authors":"Silvia Del V Alonso, F Luis González Flecha","doi":"10.1007/s12551-023-01114-0","DOIUrl":"10.1007/s12551-023-01114-0","url":null,"abstract":"<p><p>In 1972, a group of young Argentinean scientists nucleated in the so-called Membrane Club constituted the Biophysical Society of Argentina (SAB). Over the years, this Society has grown and embraced new areas of research and emerging technologies. In this commentary, we provide an overview of the early stages of biophysics development in Argentina and highlight some of the notable achievements made during the past five decades. The SAB Annual Meetings have been a platform for intense scientific discussions, and the Society has fostered numerous international connections, becoming a hallmark of SAB activities over these 50 years. Initially centered on membrane biophysics, SAB focus has since expanded to encompass diverse fields such as molecular, cellular, and systems biophysics.</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":null,"pages":null},"PeriodicalIF":4.9,"publicationDate":"2023-08-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10480372/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10245706","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}
Biophysical reviewsPub Date : 2023-08-22eCollection Date: 2023-08-01DOI: 10.1007/s12551-023-01119-9
Silvia Del Valle Alonso, Rosangela Itri, Leandro R S Barbosa, R Daniel Peluffo, F Luis González Flecha
{"title":"The Latin American Federation of Biophysical Societies (LAFeBS).","authors":"Silvia Del Valle Alonso, Rosangela Itri, Leandro R S Barbosa, R Daniel Peluffo, F Luis González Flecha","doi":"10.1007/s12551-023-01119-9","DOIUrl":"10.1007/s12551-023-01119-9","url":null,"abstract":"<p><p>The Latin American Federation of Biophysical Societies (LAFeBS) was constituted in 2007 in Montevideo, Uruguay, as a collaborative effort among the Biophysical Societies of Argentina, Brazil, and Uruguay. This visionary collaboration foresees the future of Biophysics in Latin America. In this commentary, we will briefly review the history of LAFeBS, the remarkable path undertaken since its foundation 16 years ago, and its key initiative, the Latin American Postgraduate Program in Biophysics (POSLATAM).</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":null,"pages":null},"PeriodicalIF":4.9,"publicationDate":"2023-08-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10480359/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10560242","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}
Biophysical reviewsPub Date : 2023-08-18eCollection Date: 2023-10-01DOI: 10.1007/s12551-023-01115-z
Galina Yu Lomakina, Natalia N Ugarova
{"title":"<i>Luciola mingrelica</i> firefly luciferase as a marker in bioluminescent immunoassays.","authors":"Galina Yu Lomakina, Natalia N Ugarova","doi":"10.1007/s12551-023-01115-z","DOIUrl":"10.1007/s12551-023-01115-z","url":null,"abstract":"<p><p>Chemical modification of the enzymes with biospecific macromolecules is used in various fields of biotechnology to impart new functions or improve their properties and is a fast and convenient way to get the final products. The preparation of highly active, stable, and functionally active conjugates of the thermostable luciferase through the NH<sub>2</sub>-groups or free SH-groups of the enzyme with target molecules of different molecular weight (albumin, avidin from chicken eggs, antibodies, and progesterone) is described. The obtained conjugates were successfully tested as a reporter in bioluminescent immunoassay for the detection of the molecules and pathogens. Thus, the luc-albumin (Luc-Alb) and luc-insulin (Luc-Ins) conjugates were used in competitive ELISA for the detection of an analyte (albumin or insulin) in the samples. Luc-progesterone (Luc-Pg) was used in the rapid homogeneous immunoassay of progesterone by the BRET technique with the detection limit of 0.5 ng/ml. Luciferase conjugates with avidin (Luc-Avi) and secondary and primary antibodies (Luc-RAM and Luc-Sal) were used for enzyme immunoassay detection of <i>Salmonella paratyphi A</i> cells with the cell detection limit of 5 × 10<sup>4</sup> CFU/ml. To reduce the detection limit of <i>Salmonella</i> cells, we developed a pseudo-homogeneous bioluminescent enzyme immunoassay of cells using a new matrix for the analyte capture-polystyrene microparticles coated with Pluronic F108, covalently labeled with Sal antibodies. This allowed to achieve efficient trapping of cells from solution, significantly reduced nonspecific sorption and decreased the cell detection limit to 2.7 × 10<sup>3</sup> CFU/ml without prior concentration of the sample. The methodology that was developed in this study can be applied for the development of novel bioanalytical systems based on firefly luciferases.</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":null,"pages":null},"PeriodicalIF":4.9,"publicationDate":"2023-08-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10643422/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"46908979","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}
Biophysical reviewsPub Date : 2023-08-18eCollection Date: 2023-10-01DOI: 10.1007/s12551-023-01106-0
Veronika Kopylova, Stanislav Boronovskiy, Yaroslav Nartsissov
{"title":"Approaches to vascular network, blood flow, and metabolite distribution modeling in brain tissue.","authors":"Veronika Kopylova, Stanislav Boronovskiy, Yaroslav Nartsissov","doi":"10.1007/s12551-023-01106-0","DOIUrl":"10.1007/s12551-023-01106-0","url":null,"abstract":"<p><p>The cardiovascular system plays a key role in the transport of nutrients, ensuring a continuous supply of all cells of the body with the metabolites necessary for life. The blood supply to the brain is carried out by the large arteries located on its surface, which branch into smaller arterioles that penetrate the cerebral cortex and feed the capillary bed, thereby forming an extensive branching network. The formation of blood vessels is carried out via vasculogenesis and angiogenesis, which play an important role in both embryo and adult life. The review presents approaches to modeling various aspects of both the formation of vascular networks and the construction of the formed arterial tree. In addition, a brief description of models that allows one to study the blood flow in various parts of the circulatory system and the spatiotemporal metabolite distribution in brain tissues is given. Experimental study of these issues is not always possible due to both the complexity of the cardiovascular system and the mechanisms through which the perfusion of all body cells is carried out. In this regard, mathematical models are a good tool for studying hemodynamics and can be used in clinical practice to diagnose vascular diseases and assess the need for treatment.</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":null,"pages":null},"PeriodicalIF":4.9,"publicationDate":"2023-08-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10643724/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"43220443","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}
Biophysical reviewsPub Date : 2023-08-18eCollection Date: 2023-10-01DOI: 10.1007/s12551-023-01109-x
T Yu Fufina, L G Vasilieva
{"title":"Role of hydrogen-bond networks on the donor side of photosynthetic reaction centers from purple bacteria.","authors":"T Yu Fufina, L G Vasilieva","doi":"10.1007/s12551-023-01109-x","DOIUrl":"10.1007/s12551-023-01109-x","url":null,"abstract":"<p><p>For the last decades, significant progress has been made in studying the biological functions of H-bond networks in membrane proteins, proton transporters, receptors, and photosynthetic reaction centers. Increasing availability of the X-ray crystal and cryo-electron microscopy structures of photosynthetic complexes resolved with high atomic resolution provides a platform for their comparative analysis. It allows identifying structural factors that are ensuring the high quantum yield of the photochemical reactions and are responsible for the stability of the membrane complexes. The H-bond networks are known to be responsible for proton transport associated with electron transfer from the primary to the secondary quinone as well as in the processes of water oxidation in photosystem II. Participation of such networks in reactions proceeding on the periplasmic side of bacterial photosynthetic reaction centers is less studied. This review summarizes the current understanding of the role of H-bond networks on the donor side of photosynthetic reaction centers from purple bacteria. It is discussed that the networks may be involved in providing close association with mobile electron carriers, in light-induced proton transport, in regulation of the redox properties of bacteriochlorophyll cofactors, and in stabilization of the membrane protein structure at the interface of membrane and soluble phases.</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":null,"pages":null},"PeriodicalIF":4.9,"publicationDate":"2023-08-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10643783/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"48017341","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}
Biophysical reviewsPub Date : 2023-08-17eCollection Date: 2023-08-01DOI: 10.1007/s12551-023-01101-5
J Jeremías Incicco, Leila A Cababie, Carolina Sarto, Natalia S Adler, Fernando Amrein, Evelyn Mikkelsen, Mehrnoosh Arrar, Sergio B Kaufman
{"title":"Thermodynamic and mechanistic analysis of the functional properties of dengue virus NS3 helicase.","authors":"J Jeremías Incicco, Leila A Cababie, Carolina Sarto, Natalia S Adler, Fernando Amrein, Evelyn Mikkelsen, Mehrnoosh Arrar, Sergio B Kaufman","doi":"10.1007/s12551-023-01101-5","DOIUrl":"10.1007/s12551-023-01101-5","url":null,"abstract":"<p><p>The Dengue Virus (DENV) non-structural protein 3 (NS3) is a multi-functional protein critical in the viral life cycle. The DENV NS3 is comprised of a serine protease domain and a helicase domain. The helicase domain itself acts as a molecular motor, either translocating in a unidirectional manner along single-stranded RNA or unwinding double-stranded RNA, processes fueled by the hydrolysis of nucleoside triphosphates. In this brief review, we summarize our contributions and ongoing efforts to uncover the thermodynamic and mechanistic functional properties of the DENV NS3 as an NTPase and helicase.</p>","PeriodicalId":9094,"journal":{"name":"Biophysical reviews","volume":null,"pages":null},"PeriodicalIF":4.9,"publicationDate":"2023-08-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10480135/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10180611","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}