Annual Review of Biophysics最新文献

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Temperature, Dynamics, and Enzyme-Catalyzed Reaction Rates. 温度、动力学和酶催化反应速率。
IF 12.4 1区 生物学
Annual Review of Biophysics Pub Date : 2020-05-06 DOI: 10.1146/annurev-biophys-121219-081520
Vickery L Arcus, Adrian J Mulholland
{"title":"Temperature, Dynamics, and Enzyme-Catalyzed Reaction Rates.","authors":"Vickery L Arcus, Adrian J Mulholland","doi":"10.1146/annurev-biophys-121219-081520","DOIUrl":"https://doi.org/10.1146/annurev-biophys-121219-081520","url":null,"abstract":"We review the adaptations of enzyme activity to different temperatures. Psychrophilic (cold-adapted) enzymes show significantly different activation parameters (lower activation enthalpies and entropies) than their mesophilic counterparts. Furthermore, there is increasing evidence that the temperature dependence of many enzyme-catalyzed reactions is more complex than is widely believed. Many enzymes show curvature in plots of activity versus temperature that is not accounted for by denaturation or unfolding. This is explained by macromolecular rate theory: A negative activation heat capacity for the rate-limiting chemical step leads directly to predictions of temperature optima; both entropy and enthalpy are temperature dependent. Fluctuations in the transition state ensemble are reduced compared to the ground state. We show how investigations combining experiment with molecular simulation are revealing fundamental details of enzyme thermoadaptation that are relevant for understanding aspects of enzyme evolution. Simulations can calculate relevant thermodynamic properties (such as activation enthalpies, entropies, and heat capacities) and reveal the molecular mechanisms underlying experimentally observed behavior. Expected final online publication date for the Annual Review of Biophysics, Volume 49 is May 6, 2020. Please see http://www.annualreviews.org/page/journal/pubdates for revised estimates.","PeriodicalId":50756,"journal":{"name":"Annual Review of Biophysics","volume":"49 ","pages":"163-180"},"PeriodicalIF":12.4,"publicationDate":"2020-05-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev-biophys-121219-081520","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9146131","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"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: 44
RNA-Mediated Virus Assembly: Mechanisms and Consequences for Viral Evolution and Therapy. rna介导的病毒组装:病毒进化和治疗的机制和后果。
IF 12.4 1区 生物学
Annual Review of Biophysics Pub Date : 2019-05-06 DOI: 10.1146/annurev-biophys-052118-115611
Reidun Twarock, Peter G Stockley
{"title":"RNA-Mediated Virus Assembly: Mechanisms and Consequences for Viral Evolution and Therapy.","authors":"Reidun Twarock,&nbsp;Peter G Stockley","doi":"10.1146/annurev-biophys-052118-115611","DOIUrl":"https://doi.org/10.1146/annurev-biophys-052118-115611","url":null,"abstract":"<p><p>Viruses, entities composed of nucleic acids, proteins, and in some cases lipids lack the ability to replicate outside their target cells. Their components self-assemble at the nanoscale with exquisite precision-a key to their biological success in infection. Recent advances in structure determination and the development of biophysical tools such as single-molecule spectroscopy and noncovalent mass spectrometry allow unprecedented access to the detailed assembly mechanisms of simple virions. Coupling these techniques with mathematical modeling and bioinformatics has uncovered a previously unsuspected role for genomic RNA in regulating formation of viral capsids, revealing multiple, dispersed RNA sequence/structure motifs [packaging signals (PSs)] that bind cognate coat proteins cooperatively. The PS ensemble controls assembly efficiency and accounts for the packaging specificity seen in vivo. The precise modes of action of the PSs vary between viral families, but this common principle applies across many viral families, including major human pathogens. These insights open up the opportunity to block or repurpose PS function in assembly for both novel antiviral therapy and gene/drug/vaccine applications.</p>","PeriodicalId":50756,"journal":{"name":"Annual Review of Biophysics","volume":"48 ","pages":"495-514"},"PeriodicalIF":12.4,"publicationDate":"2019-05-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev-biophys-052118-115611","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9103478","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"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: 50
Hydrogel-Tissue Chemistry: Principles and Applications. 水凝胶-组织化学:原理和应用。
IF 12.4 1区 生物学
Annual Review of Biophysics Pub Date : 2018-05-20 DOI: 10.1146/annurev-biophys-070317-032905
Viviana Gradinaru, Jennifer Treweek, Kristin Overton, Karl Deisseroth
{"title":"Hydrogel-Tissue Chemistry: Principles and Applications.","authors":"Viviana Gradinaru,&nbsp;Jennifer Treweek,&nbsp;Kristin Overton,&nbsp;Karl Deisseroth","doi":"10.1146/annurev-biophys-070317-032905","DOIUrl":"https://doi.org/10.1146/annurev-biophys-070317-032905","url":null,"abstract":"<p><p>Over the past five years, a rapidly developing experimental approach has enabled high-resolution and high-content information retrieval from intact multicellular animal (metazoan) systems. New chemical and physical forms are created in the hydrogel-tissue chemistry process, and the retention and retrieval of crucial phenotypic information regarding constituent cells and molecules (and their joint interrelationships) are thereby enabled. For example, rich data sets defining both single-cell-resolution gene expression and single-cell-resolution activity during behavior can now be collected while still preserving information on three-dimensional positioning and/or brain-wide wiring of those very same neurons-even within vertebrate brains. This new approach and its variants, as applied to neuroscience, are beginning to illuminate the fundamental cellular and chemical representations of sensation, cognition, and action. More generally, reimagining metazoans as metareactants-or positionally defined three-dimensional graphs of constituent chemicals made available for ongoing functionalization, transformation, and readout-is stimulating innovation across biology and medicine.</p>","PeriodicalId":50756,"journal":{"name":"Annual Review of Biophysics","volume":"47 ","pages":"355-376"},"PeriodicalIF":12.4,"publicationDate":"2018-05-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev-biophys-070317-032905","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9340255","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"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: 90
The Biophysics of 3D Cell Migration 三维细胞迁移的生物物理学
IF 12.4 1区 生物学
Annual Review of Biophysics Pub Date : 2018-05-20 DOI: 10.1146/ANNUREV-BIOPHYS-070816-033854
Pei-Hsun Wu, Daniele M. Gilkes, D. Wirtz
{"title":"The Biophysics of 3D Cell Migration","authors":"Pei-Hsun Wu, Daniele M. Gilkes, D. Wirtz","doi":"10.1146/ANNUREV-BIOPHYS-070816-033854","DOIUrl":"https://doi.org/10.1146/ANNUREV-BIOPHYS-070816-033854","url":null,"abstract":"Three-dimensional (3D) cell culture systems have gained increasing interest not only for 3D migration studies but also for their use in drug screening, tissue engineering, and ex vivo modeling of m...","PeriodicalId":50756,"journal":{"name":"Annual Review of Biophysics","volume":"47 1","pages":"549-567"},"PeriodicalIF":12.4,"publicationDate":"2018-05-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/ANNUREV-BIOPHYS-070816-033854","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"46708460","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"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: 34
Mechanotransduction by the Actin Cytoskeleton: Converting Mechanical Stimuli into Biochemical Signals 肌动蛋白细胞骨架的机械转导:将机械刺激转化为生化信号
IF 12.4 1区 生物学
Annual Review of Biophysics Pub Date : 2018-05-20 DOI: 10.1146/ANNUREV-BIOPHYS-070816-033547
A. Harris, P. Jreij, D. Fletcher
{"title":"Mechanotransduction by the Actin Cytoskeleton: Converting Mechanical Stimuli into Biochemical Signals","authors":"A. Harris, P. Jreij, D. Fletcher","doi":"10.1146/ANNUREV-BIOPHYS-070816-033547","DOIUrl":"https://doi.org/10.1146/ANNUREV-BIOPHYS-070816-033547","url":null,"abstract":"Force transmission through the actin cytoskeleton plays a central role in cell movements, shape change, and internal organization. Dynamic reorganization of actin filaments by an array of specializ...","PeriodicalId":50756,"journal":{"name":"Annual Review of Biophysics","volume":"47 1","pages":"617-631"},"PeriodicalIF":12.4,"publicationDate":"2018-05-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/ANNUREV-BIOPHYS-070816-033547","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"45064480","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"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: 82
Soft Matter in Lipid-Protein Interactions. 脂质-蛋白相互作用中的软物质。
IF 12.4 1区 生物学
Annual Review of Biophysics Pub Date : 2017-05-22 DOI: 10.1146/annurev-biophys-070816-033843
Michael F Brown
{"title":"Soft Matter in Lipid-Protein Interactions.","authors":"Michael F Brown","doi":"10.1146/annurev-biophys-070816-033843","DOIUrl":"https://doi.org/10.1146/annurev-biophys-070816-033843","url":null,"abstract":"<p><p>Membrane lipids and cellular water (soft matter) are becoming increasingly recognized as key determinants of protein structure and function. Their influences can be ascribed to modulation of the bilayer properties or to specific binding and allosteric regulation of protein activity. In this review, we first consider hydrophobic matching of the intramembranous proteolipid boundary to explain the conformational changes and oligomeric states of proteins within the bilayer. Alternatively, membranes can be viewed as complex fluids, whose properties are linked to key biological functions. Critical behavior and nonideal mixing of the lipids have been proposed to explain how raft-like microstructures involving cholesterol affect membrane protein activity. Furthermore, the persistence length for lipid-protein interactions suggests the curvature force field of the membrane comes into play. A flexible surface model describes how curvature and hydrophobic forces lead to the emergence of new protein functional states within the membrane lipid bilayer.</p>","PeriodicalId":50756,"journal":{"name":"Annual Review of Biophysics","volume":"46 ","pages":"379-410"},"PeriodicalIF":12.4,"publicationDate":"2017-05-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev-biophys-070816-033843","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10075421","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"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: 89
Structural Insights into the Eukaryotic Transcription Initiation Machinery. 真核生物转录启动机制的结构透视。
IF 10.4 1区 生物学
Annual Review of Biophysics Pub Date : 2017-05-22 DOI: 10.1146/annurev-biophys-070816-033751
Eva Nogales, Robert K Louder, Yuan He
{"title":"Structural Insights into the Eukaryotic Transcription Initiation Machinery.","authors":"Eva Nogales, Robert K Louder, Yuan He","doi":"10.1146/annurev-biophys-070816-033751","DOIUrl":"10.1146/annurev-biophys-070816-033751","url":null,"abstract":"<p><p>Eukaryotic gene transcription requires the assembly at the promoter of a large preinitiation complex (PIC) that includes RNA polymerase II (Pol II) and the general transcription factors TFIID, TFIIA, TFIIB, TFIIF, TFIIE, and TFIIH. The size and complexity of Pol II, TFIID, and TFIIH have precluded their reconstitution from heterologous systems, and purification relies on scarce endogenous sources. Together with their conformational flexibility and the transient nature of their interactions, these limitations had precluded structural characterization of the PIC. In the last few years, however, progress in cryo-electron microscopy (cryo-EM) has made possible the visualization, at increasingly better resolution, of large PIC assemblies in different functional states. These structures can now be interpreted in near-atomic detail and provide an exciting structural framework for past and future functional studies, giving us unique mechanistic insight into the complex process of transcription initiation.</p>","PeriodicalId":50756,"journal":{"name":"Annual Review of Biophysics","volume":"46 ","pages":"59-83"},"PeriodicalIF":10.4,"publicationDate":"2017-05-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6186020/pdf/nihms-991452.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10732778","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"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
Mechanisms of ATP-Dependent Chromatin Remodeling Motors. atp依赖性染色质重塑马达的机制。
IF 12.4 1区 生物学
Annual Review of Biophysics Pub Date : 2016-07-05 DOI: 10.1146/annurev-biophys-051013-022819
Coral Y Zhou, Stephanie L Johnson, Nathan I Gamarra, Geeta J Narlikar
{"title":"Mechanisms of ATP-Dependent Chromatin Remodeling Motors.","authors":"Coral Y Zhou,&nbsp;Stephanie L Johnson,&nbsp;Nathan I Gamarra,&nbsp;Geeta J Narlikar","doi":"10.1146/annurev-biophys-051013-022819","DOIUrl":"https://doi.org/10.1146/annurev-biophys-051013-022819","url":null,"abstract":"<p><p>Chromatin remodeling motors play essential roles in all DNA-based processes. These motors catalyze diverse outcomes ranging from sliding the smallest units of chromatin, known as nucleosomes, to completely disassembling chromatin. The broad range of actions carried out by these motors on the complex template presented by chromatin raises many stimulating mechanistic questions. Other well-studied nucleic acid motors provide examples of the depth of mechanistic understanding that is achievable from detailed biophysical studies. We use these studies as a guiding framework to discuss the current state of knowledge of chromatin remodeling mechanisms and highlight exciting open questions that would continue to benefit from biophysical analyses.</p>","PeriodicalId":50756,"journal":{"name":"Annual Review of Biophysics","volume":"45 ","pages":"153-81"},"PeriodicalIF":12.4,"publicationDate":"2016-07-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev-biophys-051013-022819","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10592736","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"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: 115
Regulation of Rad6/Rad18 Activity During DNA Damage Tolerance. DNA 损伤耐受过程中 Rad6/Rad18 活性的调控
IF 12.4 1区 生物学
Annual Review of Biophysics Pub Date : 2015-01-01 DOI: 10.1146/annurev-biophys-060414-033841
Mark Hedglin, Stephen J Benkovic
{"title":"Regulation of Rad6/Rad18 Activity During DNA Damage Tolerance.","authors":"Mark Hedglin, Stephen J Benkovic","doi":"10.1146/annurev-biophys-060414-033841","DOIUrl":"10.1146/annurev-biophys-060414-033841","url":null,"abstract":"<p><p>Replicative polymerases (pols) cannot accommodate damaged template bases, and these pols stall when such offenses are encountered during S phase. Rather than repairing the damaged base, replication past it may proceed via one of two DNA damage tolerance (DDT) pathways, allowing replicative DNA synthesis to resume. In translesion DNA synthesis (TLS), a specialized TLS pol is recruited to catalyze stable, yet often erroneous, nucleotide incorporation opposite damaged template bases. In template switching, the newly synthesized sister strand is used as a damage-free template to synthesize past the lesion. In eukaryotes, both pathways are regulated by the conjugation of ubiquitin to the PCNA sliding clamp by distinct E2/E3 pairs. Whereas monoubiquitination by Rad6/Rad18 mediates TLS, extension of this ubiquitin to a polyubiquitin chain by Ubc13-Mms2/Rad5 routes DDT to the template switching pathway. In this review, we focus on the monoubiquitination of PCNA by Rad6/Rad18 and summarize the current knowledge of how this process is regulated. </p>","PeriodicalId":50756,"journal":{"name":"Annual Review of Biophysics","volume":"44 ","pages":"207-28"},"PeriodicalIF":12.4,"publicationDate":"2015-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5592839/pdf/nihms902161.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33409760","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"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
Structural Symmetry in Membrane Proteins. 膜蛋白的结构对称性。
IF 12.4 1区 生物学
Annual Review of Biophysics Pub Date : 2015-01-01 DOI: 10.1146/annurev-biophys-051013-023008
Lucy R Forrest
{"title":"Structural Symmetry in Membrane Proteins.","authors":"Lucy R Forrest","doi":"10.1146/annurev-biophys-051013-023008","DOIUrl":"https://doi.org/10.1146/annurev-biophys-051013-023008","url":null,"abstract":"<p><p>Symmetry is a common feature among natural systems, including protein structures. A strong propensity toward symmetric architectures has long been recognized for water-soluble proteins, and this propensity has been rationalized from an evolutionary standpoint. Proteins residing in cellular membranes, however, have traditionally been less amenable to structural studies, and thus the prevalence and significance of symmetry in this important class of molecules is not as well understood. In the past two decades, researchers have made great strides in this area, and these advances have provided exciting insights into the range of architectures adopted by membrane proteins. These structural studies have revealed a similarly strong bias toward symmetric arrangements, which were often unexpected and which occurred despite the restrictions imposed by the membrane environment on the possible symmetry groups. Moreover, membrane proteins disproportionately contain internal structural repeats resulting from duplication and fusion of smaller segments. This article discusses the types and origins of symmetry in membrane proteins and the implications of symmetry for protein function. </p>","PeriodicalId":50756,"journal":{"name":"Annual Review of Biophysics","volume":"44 ","pages":"311-37"},"PeriodicalIF":12.4,"publicationDate":"2015-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev-biophys-051013-023008","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33409763","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"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: 114
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