Quarterly Reviews of Biophysics最新文献

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Digging into the biophysical features of cell membranes with lipid-DNA conjugates. 利用脂质-DNA 共轭物挖掘细胞膜的生物物理特征。
IF 7.2 2区 生物学
Quarterly Reviews of Biophysics Pub Date : 2022-05-16 DOI: 10.1017/S003358352200004X
Ahsan Ausaf Ali, Yousef Bagheri, Mingxu You
{"title":"Digging into the biophysical features of cell membranes with lipid-DNA conjugates.","authors":"Ahsan Ausaf Ali, Yousef Bagheri, Mingxu You","doi":"10.1017/S003358352200004X","DOIUrl":"10.1017/S003358352200004X","url":null,"abstract":"<p><p>Lipid-DNA conjugates have emerged as highly useful tools to modify the cell membranes. These conjugates generally consist of a lipid anchor for membrane modification and a functional DNA nanostructure for membrane analysis or regulation. There are several unique properties of these lipid-DNA conjugates, especially including their programmability, fast and efficient membrane insertion, and precise sequence-specific assembly. These unique properties have enabled a broad range of biophysical applications on live cell membranes. In this review, we will mainly focus on recent tremendous progress, especially during the past three years, in regulating the biophysical features of these lipid-DNA conjugates and their key applications in studying cell membrane biophysics. Some insights into the current challenges and future directions of this interdisciplinary field have also been provided.</p>","PeriodicalId":20828,"journal":{"name":"Quarterly Reviews of Biophysics","volume":null,"pages":null},"PeriodicalIF":7.2,"publicationDate":"2022-05-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9284422/pdf/nihms-1821360.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9824987","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
The use of vector formalism in the analysis of hydrophobic and electric driving forces in biological assemblies. 利用矢量形式分析生物组装中的疏水和电驱动力。
IF 6.1 2区 生物学
Quarterly Reviews of Biophysics Pub Date : 2022-04-11 DOI: 10.1017/S0033583522000038
Angel Mozo-Villarías, Juan A Cedano, Enrique Querol
{"title":"The use of vector formalism in the analysis of hydrophobic and electric driving forces in biological assemblies.","authors":"Angel Mozo-Villarías, Juan A Cedano, Enrique Querol","doi":"10.1017/S0033583522000038","DOIUrl":"10.1017/S0033583522000038","url":null,"abstract":"","PeriodicalId":20828,"journal":{"name":"Quarterly Reviews of Biophysics","volume":null,"pages":null},"PeriodicalIF":6.1,"publicationDate":"2022-04-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"87765617","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Studies of cell-penetrating peptides by biophysical methods. 用生物物理方法研究细胞穿透肽。
IF 6.1 2区 生物学
Quarterly Reviews of Biophysics Pub Date : 2022-04-11 DOI: 10.1017/S0033583522000026
Matjaž Zorko, Ülo Langel
{"title":"Studies of cell-penetrating peptides by biophysical methods.","authors":"Matjaž Zorko, Ülo Langel","doi":"10.1017/S0033583522000026","DOIUrl":"10.1017/S0033583522000026","url":null,"abstract":"","PeriodicalId":20828,"journal":{"name":"Quarterly Reviews of Biophysics","volume":null,"pages":null},"PeriodicalIF":6.1,"publicationDate":"2022-04-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"84600508","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Structures of synthetic helical filaments and tubes based on peptide and peptido-mimetic polymers. 基于肽和拟肽聚合物的合成螺旋丝和管的结构。
IF 6.1 2区 生物学
Quarterly Reviews of Biophysics Pub Date : 2022-03-21 DOI: 10.1017/S0033583522000014
Jessalyn G Miller, Spencer A Hughes, Charles Modlin, Vincent P Conticello
{"title":"Structures of synthetic helical filaments and tubes based on peptide and peptido-mimetic polymers.","authors":"Jessalyn G Miller, Spencer A Hughes, Charles Modlin, Vincent P Conticello","doi":"10.1017/S0033583522000014","DOIUrl":"10.1017/S0033583522000014","url":null,"abstract":"","PeriodicalId":20828,"journal":{"name":"Quarterly Reviews of Biophysics","volume":null,"pages":null},"PeriodicalIF":6.1,"publicationDate":"2022-03-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91254790","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Differential repair enzyme-substrate selection within dynamic DNA energy landscapes. 动态DNA能量景观中的差异修复酶-底物选择。
IF 6.1 2区 生物学
Quarterly Reviews of Biophysics Pub Date : 2021-12-06 DOI: 10.1017/S0033583521000093
J Völker, K J Breslauer
{"title":"Differential repair enzyme-substrate selection within dynamic DNA energy landscapes.","authors":"J Völker,&nbsp;K J Breslauer","doi":"10.1017/S0033583521000093","DOIUrl":"https://doi.org/10.1017/S0033583521000093","url":null,"abstract":"<p><p>We demonstrate that reshaping of the dynamic, bulged-loop energy landscape of DNA triplet repeat ensembles by the presence of an abasic site alters repair outcomes by the APE1 enzyme. This phenomenon depends on the structural context of the lesion, despite the abasic site always having the same neighbors in sequence space. We employ this lesion-induced redistribution of DNA states and a kinetic trap to monitor different occupancies of the DNA bulge loop states. We show how such dynamic redistribution and associated differential occupancies of DNA states impact APE1 repair outcomes and APE1 induced interconversions. We correlate the differential biophysical properties of the dynamic, DNA ensemble states, with their ability to be recognized and processed as substrates by the APE1 DNA repair enzyme. Enzymatic digestions and biophysical characterizations reveal that APE1 cuts a fraction (10-12%) of the dynamic, rollameric substrates within the initial kinetic distribution. APE1 interactions also 'induce' rollamer redistribution from a kinetically trapped distribution to an equilibrium distribution, the latter not containing viable APE1 substrates. We distinguish between kinetically controlled ensemble (re)distributions of potential DNA substrates, versus thermodynamically controlled ensemble (re)distribution; features of importance to DNA regulation. We conclude that APE1 activity catalyzes/induces ensembles that represent the thermodynamically optimal loop distribution, yet which also are nonviable substrate states for abasic site cleavage by APE1. We propose that by inducing substrate redistributions in a dynamic energy landscape, the enzyme actually reduces the available substrate competent species for it to process, reflective of a regulatory mechanism for enzymatic self-repression. If this is a general phenomenon, such a consequence would have a profound impact on slowing down and/or misdirecting DNA repair within dynamic energy landscapes, as exemplified here within triplet repeat domains. In short, APE1-instigated redistribution of potential substrates induces a preferred pathway to an equilibrium ensemble of enzymatically incompetent states.</p>","PeriodicalId":20828,"journal":{"name":"Quarterly Reviews of Biophysics","volume":null,"pages":null},"PeriodicalIF":6.1,"publicationDate":"2021-12-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39945924","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 4
The mechanics of mitotic chromosomes. 有丝分裂染色体的机制。
IF 6.1 2区 生物学
Quarterly Reviews of Biophysics Pub Date : 2021-09-17 DOI: 10.1017/S0033583521000081
T Man, H Witt, E J G Peterman, G J L Wuite
{"title":"The mechanics of mitotic chromosomes.","authors":"T Man,&nbsp;H Witt,&nbsp;E J G Peterman,&nbsp;G J L Wuite","doi":"10.1017/S0033583521000081","DOIUrl":"https://doi.org/10.1017/S0033583521000081","url":null,"abstract":"<p><p>Condensation and faithful separation of the genome are crucial for the cellular life cycle. During chromosome segregation, mechanical forces generated by the mitotic spindle pull apart the sister chromatids. The mechanical nature of this process has motivated a lot of research interest into the mechanical properties of mitotic chromosomes. Although their fundamental mechanical characteristics are known, it still remains unclear how these characteristics emerge from the structure of the mitotic chromosome. Recent advances in genomics, computational and super-resolution microscopy techniques have greatly promoted our understanding of the chromosomal structure and have motivated us to review the mechanical characteristics of chromosomes in light of the current structural insights. In this review, we will first introduce the current understanding of the chromosomal structure, before reviewing characteristic mechanical properties such as the Young's modulus and the bending modulus of mitotic chromosomes. Then we will address the approaches used to relate mechanical properties to the structure of chromosomes and we will also discuss how mechanical characterization can aid in elucidating their structure. Finally, future challenges, recent developments and emergent questions in this research field will be discussed.</p>","PeriodicalId":20828,"journal":{"name":"Quarterly Reviews of Biophysics","volume":null,"pages":null},"PeriodicalIF":6.1,"publicationDate":"2021-09-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39423350","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 4
A molecular view of DNA flexibility. DNA柔韧性的分子观。
IF 6.1 2区 生物学
Quarterly Reviews of Biophysics Pub Date : 2021-07-06 DOI: 10.1017/S0033583521000068
Alberto Marin-Gonzalez, J G Vilhena, Ruben Perez, Fernando Moreno-Herrero
{"title":"A molecular view of DNA flexibility.","authors":"Alberto Marin-Gonzalez,&nbsp;J G Vilhena,&nbsp;Ruben Perez,&nbsp;Fernando Moreno-Herrero","doi":"10.1017/S0033583521000068","DOIUrl":"https://doi.org/10.1017/S0033583521000068","url":null,"abstract":"<p><p>DNA dynamics can only be understood by taking into account its complex mechanical behavior at different length scales. At the micrometer level, the mechanical properties of single DNA molecules have been well-characterized by polymer models and are commonly quantified by a persistence length of 50 nm (~150 bp). However, at the base pair level (~3.4 Å), the dynamics of DNA involves complex molecular mechanisms that are still being deciphered. Here, we review recent single-molecule experiments and molecular dynamics simulations that are providing novel insights into DNA mechanics from such a molecular perspective. We first discuss recent findings on sequence-dependent DNA mechanical properties, including sequences that resist mechanical stress and sequences that can accommodate strong deformations. We then comment on the intricate effects of cytosine methylation and DNA mismatches on DNA mechanics. Finally, we review recently reported differences in the mechanical properties of DNA and double-stranded RNA, the other double-helical carrier of genetic information. A thorough examination of the recent single-molecule literature permits establishing a set of general 'rules' that reasonably explain the mechanics of nucleic acids at the base pair level. These simple rules offer an improved description of certain biological systems and might serve as valuable guidelines for future design of DNA and RNA nanostructures.</p>","PeriodicalId":20828,"journal":{"name":"Quarterly Reviews of Biophysics","volume":null,"pages":null},"PeriodicalIF":6.1,"publicationDate":"2021-07-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1017/S0033583521000068","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39151818","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 19
Where in the cell is my protein? 我的蛋白质在细胞的什么地方?
IF 6.1 2区 生物学
Quarterly Reviews of Biophysics Pub Date : 2021-06-21 DOI: 10.1017/S003358352100007X
David J DeRosier
{"title":"Where in the cell is my protein?","authors":"David J DeRosier","doi":"10.1017/S003358352100007X","DOIUrl":"https://doi.org/10.1017/S003358352100007X","url":null,"abstract":"<p><p>The application of cryo-correlative light and cryo-electron microscopy (cryo-CLEM) gives us a way to locate structures of interest in the electron microscope. In brief, the structures of interest are fluorescently tagged, and images from the cryo-fluorescent microscope (cryo-FM) maps are superimposed on those from the cryo-electron microscope (cryo-EM). By enhancing cryo-FM to include single-molecule localization microscopy (SMLM), we can achieve much better localization. The introduction of cryo-SMLM increased the yield of photons from fluorophores, which can benefit localization efforts. Dahlberg and Moerner (2021, Annual Review of Physical Chemistry, 72, 253-278) have a recent broad and elegant review of super-resolution cryo-CLEM. This paper focuses on cryo(F)PALM/STORM for the cryo-electron tomography community. I explore the current challenges to increase the accuracy of localization by SMLM and the mapping of those positions onto cryo-EM images and maps. There is much to consider: we need to know if the excitation of fluorophores damages the structures we seek to visualize. We need to determine if higher numerical aperture (NA) objectives, which add complexity to image analysis but increase resolution and the efficiency of photon collection, are better than lower NA objectives, which pose fewer problems. We need to figure out the best way to determine the axial position of fluorophores. We need to have better ways of aligning maps determined by FM with those determined by EM. We need to improve the instrumentation to be easier to use, more accurate, and ice-contamination free. The bottom line is that we have more work to do.</p>","PeriodicalId":20828,"journal":{"name":"Quarterly Reviews of Biophysics","volume":null,"pages":null},"PeriodicalIF":6.1,"publicationDate":"2021-06-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1017/S003358352100007X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39022097","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 10
A quantitative model of a cooperative two-state equilibrium in DNA: experimental tests, insights, and predictions - CORRIGENDUM. DNA合作两态平衡的定量模型:实验测试,见解和预测-勘误表。
IF 6.1 2区 生物学
Quarterly Reviews of Biophysics Pub Date : 2021-05-18 DOI: 10.1017/S0033583521000056
J Michael Schurr
{"title":"A quantitative model of a cooperative two-state equilibrium in DNA: experimental tests, insights, and predictions - CORRIGENDUM.","authors":"J Michael Schurr","doi":"10.1017/S0033583521000056","DOIUrl":"https://doi.org/10.1017/S0033583521000056","url":null,"abstract":"","PeriodicalId":20828,"journal":{"name":"Quarterly Reviews of Biophysics","volume":null,"pages":null},"PeriodicalIF":6.1,"publicationDate":"2021-05-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1017/S0033583521000056","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38911717","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Amphipathic environments for determining the structure of membrane proteins by single-particle electron cryo-microscopy. 用单粒子电子冷冻显微镜测定膜蛋白结构的两亲环境。
IF 6.1 2区 生物学
Quarterly Reviews of Biophysics Pub Date : 2021-03-31 DOI: 10.1017/S0033583521000044
Christel Le Bon, Baptiste Michon, Jean-Luc Popot, Manuela Zoonens
{"title":"Amphipathic environments for determining the structure of membrane proteins by single-particle electron cryo-microscopy.","authors":"Christel Le Bon,&nbsp;Baptiste Michon,&nbsp;Jean-Luc Popot,&nbsp;Manuela Zoonens","doi":"10.1017/S0033583521000044","DOIUrl":"https://doi.org/10.1017/S0033583521000044","url":null,"abstract":"<p><p>Over the past decade, the structural biology of membrane proteins (MPs) has taken a new turn thanks to epoch-making technical progress in single-particle electron cryo-microscopy (cryo-EM) as well as to improvements in sample preparation. The present analysis provides an overview of the extent and modes of usage of the various types of surfactants for cryo-EM studies. Digitonin, dodecylmaltoside, protein-based nanodiscs, lauryl maltoside-neopentyl glycol, glyco-diosgenin, and amphipols (APols) are the most popular surfactants at the vitrification step. Surfactant exchange is frequently used between MP purification and grid preparation, requiring extensive optimization each time the study of a new MP is undertaken. The variety of both the surfactants and experimental approaches used over the past few years bears witness to the need to continue developing innovative surfactants and optimizing conditions for sample preparation. The possibilities offered by novel APols for EM applications are discussed.</p>","PeriodicalId":20828,"journal":{"name":"Quarterly Reviews of Biophysics","volume":null,"pages":null},"PeriodicalIF":6.1,"publicationDate":"2021-03-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1017/S0033583521000044","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25532624","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 12
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