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- Volume 39, 2010
Annual Review of Biophysics - Volume 39, 2010
Volume 39, 2010
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Adventures in Physical Chemistry
Vol. 39 (2010), pp. 1–21More LessMy research has included chemical physics, electron and NMR spectroscopy, membrane biophysics, and immunology. This research was curiosity driven as well as problem and technique oriented. A theoretical equation was developed for relating nuclear hyperfine splittings to electron spin distributions in free radicals. Another equation was developed to relate NMR spectra to chemical reaction rates. Early evidence for the li Read More
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Global Dynamics of Proteins: Bridging Between Structure and Function
Vol. 39 (2010), pp. 23–42More LessBiomolecular systems possess unique, structure-encoded dynamic properties that underlie their biological functions. Recent studies indicate that these dynamic properties are determined to a large extent by the topology of native contacts. In recent years, elastic network models used in conjunction with normal mode analyses have proven to be useful for elucidating the collective dynamics intrinsically accessible under na Read More
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Simplified Models of Biological Networks
Vol. 39 (2010), pp. 43–59More LessThe function of living cells is controlled by complex regulatory networks that are built of a wide diversity of interacting molecular components. The sheer size and intricacy of molecular networks of even the simplest organisms are obstacles toward understanding network functionality. This review discusses the achievements and promise of a bottom-up approach that uses well-characterized subnetworks as model systems f Read More
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Compact Intermediates in RNA Folding
Vol. 39 (2010), pp. 61–77More LessLarge noncoding RNAs fold into their biologically functional structures via compact yet disordered intermediates, which couple the stable secondary structure of the RNA with the emerging tertiary fold. The specificity of the collapse transition, which coincides with the assembly of helical domains, depends on RNA sequence and counterions. It determines the specificity of the folding pathways and the magnitude of the free energy Read More
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Nanopore Analysis of Nucleic Acids Bound to Exonucleases and Polymerases
Vol. 39 (2010), pp. 79–90More LessWhen a voltage is imposed across a thin membrane containing a nanoscopic pore, the electric field generated within the pore captures linear ionized polymers, such as nucleic acids, that are present in the solution bathing the pore. The nucleic acid molecule transiently blocks ionic current as it is translocated through the pore, and modulations of the current provide information about the structure and dynamic motion of th Read More
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Actin Dynamics: From Nanoscale to Microscale
Vol. 39 (2010), pp. 91–110More LessThe dynamic nature of actin in cells manifests itself constantly. Polymerization near the cell edge is balanced by depolymerization in the interior, externally induced actin polymerization is followed by depolymerization, and spontaneous oscillations of actin at the cell periphery are frequently seen. I discuss how mathematical modeling relates quantitative measures of actin dynamics to the rates of underlying molecular level p Read More
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Eukaryotic Mechanosensitive Channels
Vol. 39 (2010), pp. 111–137More LessMechanosensitive ion channels are gated directly by physical stimuli and transduce these stimuli into electrical signals. Several criteria must apply for a channel to be considered mechanically gated. Mechanosensitive channels from bacterial systems have met these criteria, but few eukaryotic channels have been confirmed by the same standards. Recent work has suggested or confirmed that diverse types of channels, includin Read More
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Protein Crystallization Using Microfluidic Technologies Based on Valves, Droplets, and SlipChip
Vol. 39 (2010), pp. 139–158More LessTo obtain protein crystals, researchers must search for conditions in multidimensional chemical space. Empirically, thousands of crystallization experiments are carried out to screen various precipitants at multiple concentrations. Microfluidics can manipulate fluids on a nanoliter scale, and it affects crystallization twofold. First, it miniaturizes the experiments that can currently be done on a larger scale and enables crystallizati Read More
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Theoretical Perspectives on Protein Folding
Vol. 39 (2010), pp. 159–183More LessUnderstanding how monomeric proteins fold under in vitro conditions is crucial to describing their functions in the cellular context. Significant advances in theory and experiments have resulted in a conceptual framework for describing the folding mechanisms of globular proteins. The sizes of proteins in the denatured and folded states, cooperativity of the folding transition, dispersions in the melting temperatures at the resi Read More
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Bacterial Microcompartment Organelles: Protein Shell Structure and Evolution
Vol. 39 (2010), pp. 185–205More LessSome bacteria contain organelles or microcompartments consisting of a large virion-like protein shell encapsulating sequentially acting enzymes. These organized microcompartments serve to enhance or protect key metabolic pathways inside the cell. The variety of bacterial microcompartments provide diverse metabolic functions, ranging from CO2 fixation to the degradation of small organic molecules. Yet t Read More
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Phase Separation in Biological Membranes: Integration of Theory and Experiment
Vol. 39 (2010), pp. 207–226More LessLipid bilayer model membranes that contain a single lipid species can undergo transitions between ordered and disordered phases, and membranes that contain a mixture of lipid species can undergo phase separations. Studies of these transformations are of interest for what they can tell us about the interaction energies of lipid molecules of different species and conformations. Nanoscopic phases (<200 nm) can p Read More
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Ribosome Structure and Dynamics During Translocation and Termination
Vol. 39 (2010), pp. 227–244More LessProtein biosynthesis, or translation, occurs on the ribosome, a large RNA-protein assembly universally conserved in all forms of life. Over the last decade, structures of the small and large ribosomal subunits and of the intact ribosome have begun to reveal the molecular details of how the ribosome works. Both cryo-electron microscopy and X-ray crystallography continue to provide fresh insights into the mechanism of tran Read More
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Expanding Roles for Diverse Physical Phenomena During the Origin of Life
Vol. 39 (2010), pp. 245–263More LessRecent synthetic approaches to understanding the origin of life have yielded insights into plausible pathways for the emergence of the first cells. Here we review current experiments with implications for the origin of life, emphasizing the ability of unexpected physical processes to facilitate the self-assembly and self-replication of the first biological systems. These laboratory efforts have uncovered novel physical mechanisms for Read More
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Eukaryotic Chemotaxis: A Network of Signaling Pathways Controls Motility, Directional Sensing, and Polarity
Vol. 39 (2010), pp. 265–289More LessChemotaxis, the directed migration of cells in chemical gradients, is a vital process in normal physiology and in the pathogenesis of many diseases. Chemotactic cells display motility, directional sensing, and polarity. Motility refers to the random extension of pseudopodia, which may be driven by spontaneous actin waves that propagate through the cytoskeleton. Directional sensing is mediated by a system that detects temporal a Read More
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Protein Quantitation Using Isotope-Assisted Mass Spectrometry
Vol. 39 (2010), pp. 291–308More LessGenetic, chemical, and environmental perturbations can all induce large changes in cellular proteomes, and research aimed at quantifying these changes are an important part of modern biology. Although improvements in the hardware and software of mass spectrometers have produced increased throughput and accuracy of such measurements, new uses of heavy isotope internal standards that assist in this process hav Read More
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Structure and Activation of the Visual Pigment Rhodopsin
Vol. 39 (2010), pp. 309–328More LessRhodopsin is a specialized G protein–coupled receptor (GPCR) found in vertebrate rod cells. Absorption of light by its 11-cis retinal chromophore leads to rapid photochemical isomerization and receptor activation. Recent results from protein crystallography and NMR spectroscopy show how structural changes on the extracellular side of rhodopsin induced by retinal isomerization are coupled to the motion of membrane-span Read More
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Optical Control of Neuronal Activity
Vol. 39 (2010), pp. 329–348More LessAdvances in optics, genetics, and chemistry have enabled the investigation of brain function at all levels, from intracellular signals to single synapses, whole cells, circuits, and behavior. Until recent years, these research tools have been utilized in an observational capacity: imaging neural activity with fluorescent reporters, for example, or correlating aberrant neural activity with loss-of-function and gain-of-function pharma Read More
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Biophysics of Knotting
Vol. 39 (2010), pp. 349–366More LessKnots appear in a wide variety of biophysical systems, ranging from biopolymers, such as DNA and proteins, to macroscopic objects, such as umbilical cords and catheters. Although significant advancements have been made in the mathematical theory of knots and some progress has been made in the statistical mechanics of knots in idealized chains, the mechanisms and dynamics of knotting in biophysical systems re Read More
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Lessons Learned from UvrD Helicase: Mechanism for Directional Movement*
Vol. 39 (2010), pp. 367–385More LessHow do molecular motors convert chemical energy to mechanical work? Helicases and nucleic acids offer simple motor systems for extensive biochemical and biophysical analyses. Atomic resolution structures of UvrD-like helicases complexed with DNA in the presence of AMPPNP, ADP·Pi, and Pi reveal several salient points that aid our understanding of mechanochemical coupling. Each ATPase cycle causes two motor dom Read More
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Protein NMR Using Paramagnetic Ions
Vol. 39 (2010), pp. 387–405More LessParamagnetic metal ions offer outstanding opportunities for protein studies by nuclear magnetic resonance (NMR) spectroscopy. The paramagnetic effects manifested in the NMR spectra provide powerful restraints for the determination of the three-dimensional structure of proteins, open new possibilities for the analysis of protein-protein and protein-ligand interactions, and offer widely applicable tools for sensitivity enhanceme Read More
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Previous Volumes
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Volume 53 (2024)
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Volume 52 (2023)
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Volume 51 (2022)
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Volume 50 (2021)
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Volume 49 (2020)
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Volume 48 (2019)
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Volume 47 (2018)
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Volume 46 (2017)
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Volume 45 (2016)
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Volume 44 (2015)
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Volume 43 (2014)
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Volume 42 (2013)
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Volume 41 (2012)
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Volume 40 (2011)
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Volume 39 (2010)
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Volume 38 (2009)
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Volume 37 (2008)
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Volume 36 (2007)
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Volume 35 (2006)
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Volume 34 (2005)
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Volume 33 (2004)
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Volume 32 (2003)
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Volume 31 (2002)
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Volume 30 (2001)
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Volume 29 (2000)
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Volume 28 (1999)
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Volume 27 (1998)
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Volume 26 (1997)
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Volume 25 (1996)
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Volume 24 (1995)
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Volume 23 (1994)
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Volume 22 (1993)
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Volume 21 (1992)
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Volume 20 (1991)
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Volume 19 (1990)
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Volume 18 (1989)
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Volume 17 (1988)
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Volume 16 (1987)
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Volume 15 (1986)
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Volume 14 (1985)
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Volume 13 (1984)
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Volume 12 (1983)
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Volume 11 (1982)
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Volume 10 (1981)
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Volume 9 (1980)
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Volume 8 (1979)
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Volume 7 (1978)
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Volume 6 (1977)
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Volume 5 (1976)
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Volume 4 (1975)
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Volume 3 (1974)
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Volume 2 (1973)
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Volume 1 (1972)
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Volume 0 (1932)