Annual review of biophysics and biomolecular structure最新文献

筛选
英文 中文
Spinach on the ceiling: a theoretical chemist's return to biology. 天花板上的菠菜:一位理论化学家回归生物学。
Annual review of biophysics and biomolecular structure Pub Date : 2006-01-01 DOI: 10.1146/annurev.biophys.33.110502.133350
Martin Karplus
{"title":"Spinach on the ceiling: a theoretical chemist's return to biology.","authors":"Martin Karplus","doi":"10.1146/annurev.biophys.33.110502.133350","DOIUrl":"https://doi.org/10.1146/annurev.biophys.33.110502.133350","url":null,"abstract":"I was born in Vienna and came to the United States as a refugee in October 1938. This experience played an important role in my view of the world and my approach to science: It contributed to my realization that it was safe to stop working in fields that I felt I understood and to focus on different areas of research by asking questions that would teach me and others something new. I describe my experiences that led me from chemistry and physics back to my first love, biology, and outline some of the contributions I have made as part of my ongoing learning experience.","PeriodicalId":8270,"journal":{"name":"Annual review of biophysics and biomolecular structure","volume":"35 ","pages":"1-47"},"PeriodicalIF":0.0,"publicationDate":"2006-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.biophys.33.110502.133350","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26016801","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 44
Quantitative fluorescent speckle microscopy of cytoskeleton dynamics. 细胞骨架动力学的定量荧光散斑显微镜。
Annual review of biophysics and biomolecular structure Pub Date : 2006-01-01 DOI: 10.1146/annurev.biophys.35.040405.102114
Gaudenz Danuser, Clare M Waterman-Storer
{"title":"Quantitative fluorescent speckle microscopy of cytoskeleton dynamics.","authors":"Gaudenz Danuser,&nbsp;Clare M Waterman-Storer","doi":"10.1146/annurev.biophys.35.040405.102114","DOIUrl":"https://doi.org/10.1146/annurev.biophys.35.040405.102114","url":null,"abstract":"<p><p>Fluorescent speckle microscopy (FSM) is a technology used to analyze the dynamics of macromolecular assemblies in vivo and in vitro. Speckle formation by random association of fluorophores with a macromolecular structure was originally discovered for microtubules. Since then FSM has been expanded to study other cytoskeleton and cytoskeleton-binding proteins. Specialized software has been developed to convert the stochastic speckle image signal into spatiotemporal maps of polymer transport and turnover in living cells. These maps serve as a unique quantitative readout of the dynamic steady state of the cytoskeleton and its responses to molecular and genetic interventions, allowing a systematic study of the mechanisms of cytoskeleton regulation and its effect on cell function. Here, we explain the principles of FSM imaging and signal analysis, outline the biological questions and corresponding methodological advances that have led to the current state of FSM, and give a glimpse of new FSM modalities under development.</p>","PeriodicalId":8270,"journal":{"name":"Annual review of biophysics and biomolecular structure","volume":"35 ","pages":"361-87"},"PeriodicalIF":0.0,"publicationDate":"2006-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.biophys.35.040405.102114","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26014803","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 210
Chemical synthesis of proteins. 蛋白质的化学合成。
Annual review of biophysics and biomolecular structure Pub Date : 2005-01-01 DOI: 10.1146/annurev.biophys.34.040204.144700
Bradley L Nilsson, Matthew B Soellner, Ronald T Raines
{"title":"Chemical synthesis of proteins.","authors":"Bradley L Nilsson,&nbsp;Matthew B Soellner,&nbsp;Ronald T Raines","doi":"10.1146/annurev.biophys.34.040204.144700","DOIUrl":"https://doi.org/10.1146/annurev.biophys.34.040204.144700","url":null,"abstract":"<p><p>Proteins have become accessible targets for chemical synthesis. The basic strategy is to use native chemical ligation, Staudinger ligation, or other orthogonal chemical reactions to couple synthetic peptides. The ligation reactions are compatible with a variety of solvents and proceed in solution or on a solid support. Chemical synthesis enables a level of control on protein composition that greatly exceeds that attainable with ribosome-mediated biosynthesis. Accordingly, the chemical synthesis of proteins is providing previously unattainable insight into the structure and function of proteins.</p>","PeriodicalId":8270,"journal":{"name":"Annual review of biophysics and biomolecular structure","volume":"34 ","pages":"91-118"},"PeriodicalIF":0.0,"publicationDate":"2005-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.biophys.34.040204.144700","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25091612","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}
引用次数: 205
Modeling water, the hydrophobic effect, and ion solvation. 模拟水,疏水效应,和离子溶剂化。
Annual review of biophysics and biomolecular structure Pub Date : 2005-01-01 DOI: 10.1146/annurev.biophys.34.040204.144517
Ken A Dill, Thomas M Truskett, Vojko Vlachy, Barbara Hribar-Lee
{"title":"Modeling water, the hydrophobic effect, and ion solvation.","authors":"Ken A Dill,&nbsp;Thomas M Truskett,&nbsp;Vojko Vlachy,&nbsp;Barbara Hribar-Lee","doi":"10.1146/annurev.biophys.34.040204.144517","DOIUrl":"https://doi.org/10.1146/annurev.biophys.34.040204.144517","url":null,"abstract":"<p><p>Water plays a central role in the structures and properties of biomolecules--proteins, nucleic acids, and membranes--and in their interactions with ligands and drugs. Over the past half century, our understanding of water has been advanced significantly owing to theoretical and computational modeling. However, like the blind men and the elephant, different models describe different aspects of water's behavior. The trend in water modeling has been toward finer-scale properties and increasing structural detail, at increasing computational expense. Recently, our labs and others have moved in the opposite direction, toward simpler physical models, focusing on more global properties-water's thermodynamics, phase diagram, and solvation properties, for example-and toward less computational expense. Simplified models can guide a better understanding of water in ways that complement what we learn from more complex models. One ultimate goal is more tractable models for computer simulations of biomolecules. This review gives a perspective from simple models on how the physical properties of water-as a pure liquid and as a solvent-derive from the geometric and hydrogen bonding properties of water.</p>","PeriodicalId":8270,"journal":{"name":"Annual review of biophysics and biomolecular structure","volume":"34 ","pages":"173-99"},"PeriodicalIF":0.0,"publicationDate":"2005-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.biophys.34.040204.144517","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25090625","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 336
Paradigm shift of the plasma membrane concept from the two-dimensional continuum fluid to the partitioned fluid: high-speed single-molecule tracking of membrane molecules. 质膜概念从二维连续流体到分割流体的范式转换:膜分子的高速单分子跟踪。
Annual review of biophysics and biomolecular structure Pub Date : 2005-01-01 DOI: 10.1146/annurev.biophys.34.040204.144637
Akihiro Kusumi, Chieko Nakada, Ken Ritchie, Kotono Murase, Kenichi Suzuki, Hideji Murakoshi, Rinshi S Kasai, Junko Kondo, Takahiro Fujiwara
{"title":"Paradigm shift of the plasma membrane concept from the two-dimensional continuum fluid to the partitioned fluid: high-speed single-molecule tracking of membrane molecules.","authors":"Akihiro Kusumi,&nbsp;Chieko Nakada,&nbsp;Ken Ritchie,&nbsp;Kotono Murase,&nbsp;Kenichi Suzuki,&nbsp;Hideji Murakoshi,&nbsp;Rinshi S Kasai,&nbsp;Junko Kondo,&nbsp;Takahiro Fujiwara","doi":"10.1146/annurev.biophys.34.040204.144637","DOIUrl":"https://doi.org/10.1146/annurev.biophys.34.040204.144637","url":null,"abstract":"<p><p>Recent advancements in single-molecule tracking methods with nanometer-level precision now allow researchers to observe the movement, recruitment, and activation of single molecules in the plasma membrane in living cells. In particular, on the basis of the observations by high-speed single-particle tracking at a frame rate of 40,000 frames s(1), the partitioning of the fluid plasma membrane into submicron compartments throughout the cell membrane and the hop diffusion of virtually all the molecules have been proposed. This could explain why the diffusion coefficients in the plasma membrane are considerably smaller than those in artificial membranes, and why the diffusion coefficient is reduced upon molecular complex formation (oligomerization-induced trapping). In this review, we first describe the high-speed single-molecule tracking methods, and then we critically review a new model of a partitioned fluid plasma membrane and the involvement of the actin-based membrane-skeleton \"fences\" and anchored-transmembrane protein \"pickets\" in the formation of compartment boundaries.</p>","PeriodicalId":8270,"journal":{"name":"Annual review of biophysics and biomolecular structure","volume":"34 ","pages":"351-78"},"PeriodicalIF":0.0,"publicationDate":"2005-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.biophys.34.040204.144637","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25091039","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 1079
Membrane-protein interactions in cell signaling and membrane trafficking. 细胞信号传导和膜运输中的膜-蛋白相互作用。
Annual review of biophysics and biomolecular structure Pub Date : 2005-01-01 DOI: 10.1146/annurev.biophys.33.110502.133337
Wonhwa Cho, Robert V Stahelin
{"title":"Membrane-protein interactions in cell signaling and membrane trafficking.","authors":"Wonhwa Cho,&nbsp;Robert V Stahelin","doi":"10.1146/annurev.biophys.33.110502.133337","DOIUrl":"https://doi.org/10.1146/annurev.biophys.33.110502.133337","url":null,"abstract":"<p><p>Research in the past decade has revealed that many cytosolic proteins are recruited to different cellular membranes to form protein-protein and lipid-protein interactions during cell signaling and membrane trafficking. Membrane recruitment of these peripheral proteins is mediated by a growing number of modular membrane-targeting domains, including C1, C2, PH, FYVE, PX, ENTH, ANTH, BAR, FERM, and tubby domains, that recognize specific lipid molecules in the membranes. Structural studies of these membrane-targeting domains demonstrate how they specifically recognize their cognate lipid ligands. However, the mechanisms by which these domains and their host proteins are recruited to and interact with various cell membranes are only beginning to unravel with recent computational studies, in vitro membrane binding studies using model membranes, and cellular translocation studies using fluorescent protein-tagged proteins. This review summarizes the recent progress in our understanding of how the kinetics and energetics of membrane-protein interactions are regulated during the cellular membrane targeting and activation of peripheral proteins.</p>","PeriodicalId":8270,"journal":{"name":"Annual review of biophysics and biomolecular structure","volume":"34 ","pages":"119-51"},"PeriodicalIF":0.0,"publicationDate":"2005-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.biophys.33.110502.133337","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25091611","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 569
Toward predictive models of mammalian cells. 哺乳动物细胞的预测模型。
Annual review of biophysics and biomolecular structure Pub Date : 2005-01-01 DOI: 10.1146/annurev.biophys.34.040204.144415
Avi Ma'ayan, Robert D Blitzer, Ravi Iyengar
{"title":"Toward predictive models of mammalian cells.","authors":"Avi Ma'ayan,&nbsp;Robert D Blitzer,&nbsp;Ravi Iyengar","doi":"10.1146/annurev.biophys.34.040204.144415","DOIUrl":"https://doi.org/10.1146/annurev.biophys.34.040204.144415","url":null,"abstract":"<p><p>Progress in experimental and theoretical biology is likely to provide us with the opportunity to assemble detailed predictive models of mammalian cells. Using a functional format to describe the organization of mammalian cells, we describe current approaches for developing qualitative and quantitative models using data from a variety of experimental sources. Recent developments and applications of graph theory to biological networks are reviewed. The use of these qualitative models to identify the topology of regulatory motifs and functional modules is discussed. Cellular homeostasis and plasticity are interpreted within the framework of balance between regulatory motifs and interactions between modules. From this analysis we identify the need for detailed quantitative models on the basis of the representation of the chemistry underlying the cellular process. The use of deterministic, stochastic, and hybrid models to represent cellular processes is reviewed, and an initial integrated approach for the development of large-scale predictive models of a mammalian cell is presented.</p>","PeriodicalId":8270,"journal":{"name":"Annual review of biophysics and biomolecular structure","volume":"34 ","pages":"319-49"},"PeriodicalIF":0.0,"publicationDate":"2005-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.biophys.34.040204.144415","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25091040","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}
引用次数: 106
Single-molecule RNA science. 单分子RNA科学。
Annual review of biophysics and biomolecular structure Pub Date : 2005-01-01 DOI: 10.1146/annurev.biophys.34.040204.144641
Xiaowei Zhuang
{"title":"Single-molecule RNA science.","authors":"Xiaowei Zhuang","doi":"10.1146/annurev.biophys.34.040204.144641","DOIUrl":"https://doi.org/10.1146/annurev.biophys.34.040204.144641","url":null,"abstract":"<p><p>The development of single-molecule detection and manipulation has allowed us to monitor the behavior of individual biological molecules and molecular complexes in real time. This approach significantly expands our capability to characterize complex dynamics of biological processes, allowing transient intermediate states and parallel kinetic pathways to be directly observed. Exploring this capability to elucidate complex dynamics, recent single-molecule experiments on RNA folding and catalysis have improved our understanding of the folding energy landscape of RNA and allowed us to better dissect complex RNA catalytic reactions, including translation by the ribosome.</p>","PeriodicalId":8270,"journal":{"name":"Annual review of biophysics and biomolecular structure","volume":"34 ","pages":"399-414"},"PeriodicalIF":0.0,"publicationDate":"2005-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.biophys.34.040204.144641","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25263960","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 156
Tracking topoisomerase activity at the single-molecule level. 在单分子水平上跟踪拓扑异构酶活性。
Annual review of biophysics and biomolecular structure Pub Date : 2005-01-01 DOI: 10.1146/annurev.biophys.34.040204.144433
G Charvin, T R Strick, D Bensimon, V Croquette
{"title":"Tracking topoisomerase activity at the single-molecule level.","authors":"G Charvin,&nbsp;T R Strick,&nbsp;D Bensimon,&nbsp;V Croquette","doi":"10.1146/annurev.biophys.34.040204.144433","DOIUrl":"https://doi.org/10.1146/annurev.biophys.34.040204.144433","url":null,"abstract":"<p><p>The recent development of new techniques to manipulate single DNA molecules has opened new opportunities for the study of the enzymes that control DNA topology: the type I and II topoisomerases. These single-molecule assays provide a unique way to study the uncoiling of single supercoiled DNA molecules and the unlinking of two intertwined DNAs. They allow for a detailed characterization of the activity of topoisomerases, including the processivity, the chiral discrimination, and the dependence of their enzymatic rate on ATP concentration, degree of supercoiling, and the tension in the molecule. These results shed new light on the mechanism of these enzymes and their function in vivo.</p>","PeriodicalId":8270,"journal":{"name":"Annual review of biophysics and biomolecular structure","volume":"34 ","pages":"201-19"},"PeriodicalIF":0.0,"publicationDate":"2005-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.biophys.34.040204.144433","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25091034","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 92
Use of EPR power saturation to analyze the membrane-docking geometries of peripheral proteins: applications to C2 domains. 使用EPR功率饱和分析外周蛋白的膜对接几何形状:在C2结构域的应用。
Annual review of biophysics and biomolecular structure Pub Date : 2005-01-01 DOI: 10.1146/annurev.biophys.34.040204.144534
Nathan J Malmberg, Joseph J Falke
{"title":"Use of EPR power saturation to analyze the membrane-docking geometries of peripheral proteins: applications to C2 domains.","authors":"Nathan J Malmberg,&nbsp;Joseph J Falke","doi":"10.1146/annurev.biophys.34.040204.144534","DOIUrl":"https://doi.org/10.1146/annurev.biophys.34.040204.144534","url":null,"abstract":"<p><p>Despite the central importance of peripheral membrane proteins to cellular signaling and metabolic pathways, the structures of protein-membrane interfaces remain largely inaccessible to high-resolution structural methods. In recent years a number of laboratories have contributed to the development of an electron paramagnetic resonance (EPR) power saturation approach that utilizes site-directed spin labeling to determine the key geometric parameters of membrane-docked proteins, including their penetration depths and angular orientations relative to the membrane surface. Representative applications to Ca(2+)-activated, membrane-docking C2 domains are described.</p>","PeriodicalId":8270,"journal":{"name":"Annual review of biophysics and biomolecular structure","volume":"34 ","pages":"71-90"},"PeriodicalIF":0.0,"publicationDate":"2005-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.biophys.34.040204.144534","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25091610","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}
引用次数: 65
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
相关产品
×
本文献相关产品
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信