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- Volume 42, 2013
Annual Review of Biophysics - Volume 42, 2013
Volume 42, 2013
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Regulation of Noise in Gene Expression
Vol. 42 (2013), pp. 469–491More LessThe biochemical processes leading to the synthesis of new proteins are random, as they typically involve a small number of diffusing molecules. They lead to fluctuations in the number of proteins in a single cell as a function of time and to cell-to-cell variability of protein abundances. These in turn can lead to phenotypic heterogeneity in a population of genetically identical cells. Phenotypic heterogeneity may have important consequences for the development of multicellular organisms and the fitness of bacterial colonies, raising the question of how it is regulated. Here we review the experimental evidence that transcriptional regulation affects noise in gene expression, and discuss how the noise strength is encoded in the architecture of the promoter region. We discuss how models based on specific molecular mechanisms of gene regulation can make experimentally testable predictions for how changes to the promoter architecture are reflected in gene expression noise.
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Evolution in Microbes
Vol. 42 (2013), pp. 493–514More LessThis review presents a broad survey of experimental microbial evolution, covering diverse topics including trade-offs, epistasis, fluctuating conditions, spatial dynamics, cooperation, aging, and stochastic switching. Emphasis is placed on examples that highlight key conceptual points or address theoretical predictions. Experimental evolution is discussed from two points of view. First, population trajectories are described as adaptive walks on a fitness landscape, whose genetic structure can be probed by experiments. Second, populations are viewed from a physiological perspective, and their nongenetic heterogeneity is examined. Bringing together these two viewpoints remains a major challenge for the future.
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Protein Structure Determination by Magic-Angle Spinning Solid-State NMR, and Insights into the Formation, Structure, and Stability of Amyloid Fibrils
Vol. 42 (2013), pp. 515–536More LessProtein structure determination methods using magic-angle spinning solid-state nuclear magnetic resonance (MAS SSNMR) have experienced a remarkable development in the past decade. Significant advances in instrumentation, sample preparation, spectroscopic techniques, and computational methods have made possible the determination of the first high-resolution structures of a peptide and a protein in 2002. Subsequent developments allowed the investigation of larger proteins, the initial application of automated analysis routines, and substantial improvements in structural resolution. The application of these methods has enabled the investigation of amyloid fibril structures, conformational dynamics, and their assembly pathways at an atomic level for the first time, as these are systems not accessible by other common techniques. Recent advances and future trends for protein structure determination using MAS SSNMR, as well as its application to the study of amyloid fibrils, are reviewed.
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Structural Studies of RNase P
Vol. 42 (2013), pp. 537–557More LessRibonuclease P (RNase P) is one of the first ribozymes discovered and it is found in all phylogenetic groups. It is responsible for processing the 5′ end of pre-tRNAs as well as other RNA molecules. RNase P is formed by an RNA molecule responsible for catalysis and one or more proteins. Structural studies of the proteins from different organisms, the bacterial RNA component, and a bacterial RNase P holoenzyme/tRNA complex provide insights into the mechanism of this universal ribozyme. Together with the existing wealth of biochemical information, these studies provide atomic-level information on the mechanism of RNase P and continue to expand our understanding of the structure and architecture of large RNA molecules and ribonucleoprotein complexes, the nature of catalysis by ribozymes, the structural basis of recognition of RNA by RNA molecules, and the evolution of enzymes from the prebiotic, RNA-based world to the modern world.
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On the Universe of Protein Folds
Vol. 42 (2013), pp. 559–582More LessIn the fifty years since the first atomic structure of a protein was revealed, tens of thousands of additional structures have been solved. Like all objects in biology, proteins structures show common patterns that seem to define family relationships. Classification of proteins structures, which started in the 1970s with about a dozen structures, has continued with increasing enthusiasm, leading to two main fold classifications, SCOP and CATH, as well as many additional databases. Classification is complicated by deciding what constitutes a domain, the fundamental unit of structure. Also difficult is deciding when two given structures are similar. Like all of biology, fold classification is beset by exceptions to all rules. Thus, the perspectives of protein fold space that the fold classifications offer differ from each other. In spite of these ambiguities, fold classifications are useful for prediction of structure and function. Studying the characteristics of fold space can shed light on protein evolution and the physical laws that govern protein behavior.
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Torque Measurement at the Single-Molecule Level
Vol. 42 (2013), pp. 583–604More LessMethods for exerting and measuring forces on single molecules have revolutionized the study of the physics of biology. However, it is often the case that biological processes involve rotation or torque generation, and these parameters have been more difficult to access experimentally. Recent advances in the single-molecule field have led to the development of techniques that add the capability of torque measurement. By combining force, displacement, torque, and rotational data, a more comprehensive description of the mechanics of a biomolecule can be achieved. In this review, we highlight a number of biological processes for which torque plays a key mechanical role. We describe the various techniques that have been developed to directly probe the torque experienced by a single molecule, and detail a variety of measurements made to date using these new technologies. We conclude by discussing a number of open questions and propose systems of study that would be well suited for analysis with torsional measurement techniques.
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Modeling Gene Expression in Time and Space
Vol. 42 (2013), pp. 605–627More LessCell populations rarely exhibit gene-expression profiles that are homogeneous in time and space. In the temporal domain, dynamical behaviors such as oscillations and pulses of protein production pervade cell biology, underlying phenomena as diverse as circadian rhythmicity, cell cycle control, stress and damage responses, and stem-cell pluripotency. In multicellular populations, spatial heterogeneities are crucial for decision making and development, among many other functions. Cells need to exquisitely coordinate this temporal and spatial variation to survive. Although the spatiotemporal character of gene expression is challenging to quantify experimentally at the level of individual cells, it is beneficial from the modeling viewpoint, because it provides strong constraints that can be probed by theoretically analyzing mathematical models of candidate gene and protein circuits. Here, we review recent examples of temporal dynamics and spatial patterning in gene expression to show how modeling such phenomenology can help us unravel the molecular mechanisms of cellular function.
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Mechanics of Dynamin-Mediated Membrane Fission
Vol. 42 (2013), pp. 629–649More LessIn eukaryotic cells, membrane compartments are split into two by membrane fission. This ensures discontinuity of membrane containers and thus proper compartmentalization. The first proteic machinery implicated in catalyzing membrane fission was dynamin. Dynamin forms helical collars at the neck of endocytic buds. This structural feature suggested that the helix of dynamin could constrict in order to promote fission of the enclosed membrane. However, verifying this hypothesis revealed itself to be a challenge, which inspired many in vitro and in vivo studies. The primary goal of this review is to discuss recent structural and physical data from biophysical studies that have refined our understanding of the dynamin mechanism. In addition to the constriction hypothesis, other models have been proposed to explain how dynamin induces membrane fission. We present experimental data supporting these various models and assess which model is the most probable.
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Nanoconfinement and the Strength of Biopolymers
Vol. 42 (2013), pp. 651–673More LessThis review examines size effects observed in the mechanical strength of biopolymers that are organized in microstructures such as fibrils, layered composites, or particle nanocomposites. We review the most important aspects that connect nanoconfinement of basic material constituents at critical length scales to the mechanical performance of the entire material system: elastic modulus, strength, extensibility, and robustness. We outline theoretical and computational analysis as well as experimentation by emphasizing two strategies found in abundant natural materials: confined fibrils as part of fibers and confined mineral platelets that transfer load through a biopolymer interface in nanocomposites. We also discuss the application of confinement as a mechanism to tailor specific material properties in biological systems.
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Solid-State NMR of Nanomachines Involved in Photosynthetic Energy Conversion
Vol. 42 (2013), pp. 675–699More LessMagic-angle spinning NMR, often in combination with photo-CIDNP, is applied to determine how photosynthetic antennae and reaction centers are activated in the ground state to perform their biological function upon excitation by light. Molecular modeling resolves molecular mechanisms by way of computational integration of NMR data with other structure-function analyses. By taking evolutionary historical contingency into account, a better biophysical understanding is achieved. Chlorophyll cofactors and proteins go through self-assembly trajectories that are engineered during evolution and lead to highly homogeneous protein complexes optimized for exciton or charge transfer. Histidine-cofactor interactions allow biological nanomachines to lower energy barriers for light harvesting and charge separation in photosynthetic energy conversion. In contrast, in primordial chlorophyll antenna aggregates, excessive heterogeneity is paired with much less specific characteristics, and both exciton and charge-transfer character are encoded in the ground state.
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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)