The Current Opinion journals were developed out of the recognition that it is increasingly difficult for specialists to keep up to date with the expanding volume of information published in their subject. Elsevier’s Current Opinion journals comprise of 26 leading titles in life sciences and adjacent fields.

Current Opinion in Structural Biology

5-Year Impact Factor: 7.129
Issues per year: 6 issues
Editorial Board

Current Opinion in Structural Biology

Current Opinion in Structural Biology aims to stimulate scientifically grounded, interdisciplinary, multi-scale debate and exchange of ideas. It contains polished, concise and timely reviews and opinions, with particular emphasis on those articles published in the past two years. In addition to describing recent trends, the authors are encouraged to give their subjective opinion of the topics discussed.

In Current Opinion in Structural Biology we help the reader by providing in a systematic manner:

1. The views of experts on current advances in their field in a clear and readable form.
2. Evaluations of the most interesting papers, annotated by experts, from the great wealth of original publications.

Current Opinion in Structural Biology will serve as an invaluable source of information for researchers, lecturers, teachers, professionals, policy makers and students.

Division of the subject into sections

The subject of Structural Biology is divided into twelve themed sections, each of which is reviewed once a year. Each issue contains two sections, and the amount of space devoted to each section is related to its importance.

  • Folding and Binding
  • Nucleic acids and their protein complexes
  • Macromolecular Machines
  • Theory and Simulation
  • Sequences and Topology
  • New constructs and expression of proteins
  • Membranes
  • Engineering and Design
  • Carbohydrate-protein interactions and glycosylation
  • Biophysical and molecular biological methods
  • Multi-protein assemblies in signalling
  • Catalysis and Regulation

Selection of topics to be reviewed

Section Editors, who are major authorities in the field, are appointed by the Editors of the journal. They divide their section into a number of topics, ensuring that the field is comprehensively covered and that all issues of current importance are emphasised. Section Editors commission reviews from authorities on each topic that they have selected. The Editorial Board provides support to the Editors and the Section Editors with their comments and suggestions on names and topics.

Review articles in Current Opinion in Structural Biology are by invitation only. The journal does not accept manuscripts other from those invited by section editors, appointed by the main editors Tom Blundell and Keith Moffatt each year.

Review Articles

Authors write short review articles in which they present recent developments in their subject, emphasizing the aspects that, in their opinion, are most important. In addition, they provide short annotations to the papers that they consider to be most interesting from all those published in their topic over the previous two years.

Editorial Overview

Section Editors write a short overview at the beginning of the section to introduce the reviews and to draw the reader's attention to any particularly interesting developments.

This successful format has made Current Opinion in Structural Biology one of the most highly regarded review journals in the field with an Impact factor of 9.344.

Best Cited over the last year.

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Assessing the accuracy of physical models used in protein-folding simulations: Quantitative evidence from long molecular dynamics simulations

Advances in computer hardware, software and algorithms have now made it possible to run atomistically detailed, physics-based molecular dynamics simulations of sufficient length to observe multiple instances of protein folding and unfolding within a single equilibrium trajectory. Although such studies have already begun to provide new insights into the process of protein folding, realizing the full potential of this approach will depend not only on simulation speed, but on the accuracy of the…

Volume 24, Issue 1, 01 February 2014, Pp 98-105
Stefano Piana | John L. Klepeis | David E. Shaw

To milliseconds and beyond: Challenges in the simulation of protein folding

Quantitatively accurate all-atom molecular dynamics (MD) simulations of protein folding have long been considered a holy grail of computational biology. Due to the large system sizes and long timescales involved, such a pursuit was for many years computationally intractable. Further, sufficiently accurate forcefields needed to be developed in order to realistically model folding. This decade, however, saw the first reports of folding simulations describing kinetics on the order of milliseconds,…

Volume 23, Issue 1, 01 February 2013, Pp 58-65
Thomas J. Lane | Diwakar Shukla | Kyle A. Beauchamp | Vijay S. Pande

A new system for naming ribosomal proteins

A system for naming ribosomal proteins is described that the authors intend to use in the future. They urge others to adopt it. The objective is to eliminate the confusion caused by the assignment of identical names to ribosomal proteins from different species that are unrelated in structure and function. In the system proposed here, homologous ribosomal proteins are assigned the same name, regardless of species. It is designed so that new names are similar enough to old names to be easily…

Volume 24, Issue 1, 01 January 2014, Pp 165-169
Nenad Ban | Roland Beckmann | Jamie H.D. Cate | Jonathan D. Dinman | François Dragon | Steven R. Ellis | Denis L.J. Lafontaine | Lasse Lindahl | Anders Liljas | Jeffrey M. Lipton | Michael A. McAlear | Peter B. Moore | Harry F. Noller | Joaquin Ortega | Vikram Govind Panse | V. Ramakrishnan | Christian M.T. Spahn | Thomas A. Steitz | Marek Tchorzewski | David Tollervey | Alan J. Warren | James R. Williamson | Daniel Wilson | Ada Yonath | Marat Yusupov

Markov state models of biomolecular conformational dynamics

It has recently become practical to construct Markov state models (MSMs) that reproduce the long-time statistical conformational dynamics of biomolecules using data from molecular dynamics simulations. MSMs can predict both stationary and kinetic quantities on long timescales (e.g. milliseconds) using a set of atomistic molecular dynamics simulations that are individually much shorter, thus addressing the well-known sampling problem in molecular dynamics simulation. In addition to providing…

Volume 25, Issue , 01 January 2014, Pp 135-144
John D. Chodera | Frank Noé

Technological advances in site-directed spin labeling of proteins

Molecular flexibility over a wide time range is of central importance to the function of many proteins, both soluble and membrane. Revealing the modes of flexibility, their amplitudes, and time scales under physiological conditions is the challenge for spectroscopic methods, one of which is site-directed spin labeling EPR (SDSL-EPR). Here we provide an overview of some recent technological advances in SDSL-EPR related to investigation of structure, structural heterogeneity, and dynamics of…

Volume 23, Issue 5, 01 October 2013, Pp 725-733
Wayne L. Hubbell | Carlos J. López | Christian Altenbach | Zhongyu Yang

Single-molecule spectroscopy of protein folding dynamics-expanding scope and timescales

Single-molecule spectroscopy has developed into an important method for probing protein structure and dynamics, especially in structurally heterogeneous systems. A broad range of questions in the diversifying field of protein folding have been addressed with single-molecule Förster resonance energy transfer (FRET) and photo-induced electron transfer (PET). Building on more than a decade of rapid method development, these techniques can now be used to investigate a wide span of timescales, an…

Volume 23, Issue 1, 01 February 2013, Pp 36-47
Benjamin Schuler | Hagen Hofmann

Advances in understanding the molecular basis of plant cell wall polysaccharide recognition by carbohydrate-binding modules

Plant cell walls are complex configurations of polysaccharides that are recalcitrant to degradation. The enzymes deployed by microbes to degrade these materials comprise glycoside hydrolases, polysaccharide lyases, carbohydrate esterases and polysaccharide oxidases. Non-catalytic carbohydrate-binding modules (CBMs) are found as discretely folded units within the multi-modular structures of these enzymes where they play critical roles in the recognition of plant cell wall components and…

Volume 23, Issue 5, 01 October 2013, Pp 669-677
Harry J. Gilbert | J. Paul Knox | Alisdair B. Boraston

Impact and progress in small and wide angle X-ray scattering (SAXS and WAXS)

The advances made in small and wide angle X-ray scattering over the past decades have had a large impact on structural biology. Many new insights into challenging biological probes including large and transient complexes, flexible macromolecules as well as other exciting objects of various sizes were gained with this low resolution technique. Here, we review the recent developments in the experimental setups and in software for data collection and analysis, specifically for hybrid approaches.…

Volume 23, Issue 5, 01 October 2013, Pp 748-754
Melissa A. Graewert | Dmitri I. Svergun

Describing intrinsically disordered proteins at atomic resolution by NMR

There is growing interest in the development of physical methods to study the conformational behaviour and biological activity of intrinsically disordered proteins (IDPs). In this review recent advances in the elucidation of quantitative descriptions of disordered proteins from nuclear magnetic resonance spectroscopy are presented. Ensemble approaches are particularly well adapted to map the conformational energy landscape sampled by the protein at atomic resolution. Significant advances in…

Volume 23, Issue 3, 01 June 2013, Pp 426-435
Malene Ringkjøbing Jensen | Rob W H Ruigrok | Martin Blackledge

Structural biology in situ-the potential of subtomogram averaging

Cryo-electron tomography provides low-resolution 3D views of cells, organelles, or viruses. Macromolecular complexes present in multiple copies can be subsequently identified within the 3D reconstruction (the tomogram), computationally extracted, and averaged to obtain higher resolution 3D structures, as well as a map of their spatial distribution. This method, called subtomogram averaging or subvolume averaging, allows structures of macromolecular complexes to be resolved in situ. Recent…

Volume 23, Issue 2, 01 April 2013, Pp 261-267
John A G Briggs

Recent insights into copper-containing lytic polysaccharide mono-oxygenases

Recently the role of oxidative enzymes in the degradation of polysaccharides by saprophytic bacteria and fungi was uncovered, challenging the classical model of polysaccharide degradation of being solely via a hydrolytic pathway. 3D structural analyses of lytic polysaccharide mono-oxygenases of both bacterial AA10 (formerly CBM33) and fungal AA9 (formerly GH61) enzymes revealed structures with β-sandwich folds containing an active site with a metal coordinated by an N-terminal histidine.…

Volume 23, Issue 5, 01 October 2013, Pp 660-668
Glyn R. Hemsworth | Gideon J. Davies | Paul H. Walton

Molecular dynamics simulations of large macromolecular complexes

© 2015 Elsevier Ltd. Connecting dynamics to structural data from diverse experimental sources, molecular dynamics simulations permit the exploration of biological phenomena in unparalleled detail. Advances in simulations are moving the atomic resolution descriptions of biological systems into the million-to-billion atom regime, in which numerous cell functions reside. In this opinion, we review the progress, driven by large-scale molecular dynamics simulations, in the study of viruses,…

Volume 31, Issue , 01 April 2015, Pp 64-74
Juan R. Perilla | Boon Chong Goh | C. Keith Cassidy | Bo Liu | Rafael C. Bernardi | Till Rudack | Hang Yu | Zhe Wu | Klaus Schulten

Mass spectrometry supported determination of protein complex structure

Virtually all the biological processes are controlled and catalyzed by proteins which are, in many cases, in complexes with other proteins. Therefore, understanding the architecture and structure of protein complexes is critical to understanding their biological role and function. Traditionally, high-resolution data for structural analysis of proteins or protein complexes have been generated by the powerful methods of X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy. More…

Volume 23, Issue 2, 01 April 2013, Pp 252-260
Thomas Walzthoeni | Alexander Leitner | Florian Stengel | Ruedi Aebersold

RRM-RNA recognition: NMR or crystallography...and new findings

To characterize protein-RNA recognition at the molecular level, structural biology has turned out to be an indispensable approach. Detailed and direct insights into the mechanism of RNA binding and specificity have emerged from protein-RNA structures, especially from the most abundant RNA recognition motif (RRM). Although this protein domain has a very conserved α-β fold, it can recognize a large number of different RNA sequences and shapes and can be involved in a multitude of biological…

Volume 23, Issue 1, 01 February 2013, Pp 100-108
Gerrit M. Daubner | Antoine Cléry | Frédéric H T Allain

The dark energy of proteins comes to light: Conformational entropy and its role in protein function revealed by NMR relaxation

Historically it has been virtually impossible to experimentally determine the contribution of residual protein entropy to fundamental protein activities such as the binding of ligands. Recent progress has illuminated the possibility of employing NMR relaxation methods to quantitatively determine the role of changes in conformational entropy in molecular recognition by proteins. The method rests on using fast internal protein dynamics as a proxy. Initial results reveal a large and variable role…

Volume 23, Issue 1, 01 February 2013, Pp 75-81
A. Joshua Wand

Alternative splicing of intrinsically disordered regions and rewiring of protein interactions

Alternatively spliced protein segments tend to be intrinsically disordered and contain linear interaction motifs and/or post-translational modification sites. An emerging concept is that differential inclusion of such disordered segments can mediate new protein interactions, and hence change the context in which the biochemical or molecular functions are carried out by the protein. Since genes with disordered regions are enriched in regulatory and signaling functions, the resulting protein…

Volume 23, Issue 3, 01 June 2013, Pp 443-450
Marija Buljan | Guilhem Chalancon | A. Keith Dunker | Alex Bateman | S. Balaji | Monika Fuxreiter | M. Madan Babu

PARP-1 mechanism for coupling DNA damage detection to poly(ADP-ribose) synthesis

Poly(ADP-ribose) polymerase 1 (PARP-1) regulates gene transcription, cell death signaling, and DNA repair through production of the posttranslational modification poly(ADP-ribose). During the cellular response to genotoxic stress PARP-1 rapidly associates with DNA damage, which robustly stimulates poly(ADP-ribose) production over a low basal level of PARP-1 activity. DNA damage-dependent PARP-1 activity is central to understanding PARP-1 biological function, but structural insights into the…

Volume 23, Issue 1, 01 February 2013, Pp 134-143
Marie France Langelier | John M. Pascal

Structure- and sequence-analysis inspired engineering of proteins for enhanced thermostability

Protein engineering strategies for increasing stability can be improved by replacing random mutagenesis and high-throughput screening by approaches that include bioinformatics and computational design. Mutations can be focused on regions in the structure that are most flexible and involved in the early steps of thermal unfolding. Sequence analysis can often predict the position and nature of stabilizing mutations, and may allow the reconstruction of thermostable ancestral sequences. Various…

Volume 23, Issue 4, 01 August 2013, Pp 588-594
Hein J. Wijma | Robert J. Floor | Dick B. Janssen

Allostery without a conformational change? Revisiting the paradigm

© 2014 Elsevier Ltd. Classically, allostery induces a functional switch through a conformational change. However, lately an increasing number of studies concluded that the allostery they observe takes place through sheer dynamics. Here we explain that even if a structural comparison between the active and inactive states does not detect a conformational change, it does not mean that there is no conformational change. We list likely reasons for this lack of observation, including crystallization…

Volume 30, Issue , 01 February 2015, Pp 17-24
Ruth Nussinov | Chung Jung Tsai

Force as a single molecule probe of multidimensional protein energy landscapes

Force spectroscopy has developed into an indispensable tool for studying folding and binding of proteins on a single molecule level in real time. Design of the pulling geometry allows tuning the reaction coordinate in a very precise manner. Many recent experiments have taken advantage of this possibility and have provided detailed insight the folding pathways on the complex high dimensional energy landscape. Beyond its potential to provide control over the reaction coordinate, force is also an…

Volume 23, Issue 1, 01 February 2013, Pp 48-57
Gabriel Žoldák | Matthias Rief

Inhibition of protein aggregation and amyloid formation by small molecules

© 2014 Elsevier Ltd. For decades, drug after drug has failed to slow the progression of Alzheimer's disease in human trials. How compounds reducing fibril formation in vitro and toxicity in transgenic mice and flies bind to the Aβ toxic oligomers, is unknown. This account reviews recent drugs mainly targeting Aβ, how they were identified and report their successes from in vitro and in vivo experimental studies and their current status in clinical trials. We then focus on recent in vitro and…

Volume 30, Issue , 01 February 2015, Pp 50-56
Andrew J. Doig | Philippe Derreumaux

Advances in recombinant protein expression for use in pharmaceutical research

Protein production for structural and biophysical studies, functional assays, biomarkers, mechanistic studies in vitro and in vivo, but also for therapeutic applications in pharma, biotech and academia has evolved into a mature discipline in recent years. Due to the increased emphasis on biopharmaceuticals, the growing demand for proteins used for structural and biophysical studies, the impact of genomics technologies on the analysis of large sets of structurally diverse proteins, and the…

Volume 23, Issue 3, 01 June 2013, Pp 393-402
Rene Assenberg | Paul T. Wan | Sabine Geisse | Lorenz M. Mayr

Super-resolution fluorescence imaging with single molecules

The ability to detect, image and localize single molecules optically with high spatial precision by their fluorescence enables an emergent class of super-resolution microscopy methods which have overcome the longstanding diffraction barrier for far-fie ld light-focusing optics. Achieving spatial resolutions of 20-40. nm or better in both fixed and living cells, these methods are currently being established as powerful tools for minimally-invasive spatiotemporal analysis of structural details in…

Volume 23, Issue 5, 01 October 2013, Pp 778-787
Steffen J. Sahl | W. E. Moerner

Coarse-grain modelling of protein-protein interactions

Here, we review recent advances towards the modelling of protein-protein interactions (PPI) at the coarse-grained (CG) level, a technique that is now widely used to understand protein affinity, aggregation and self-assembly behaviour. PPI models of soluble proteins and membrane proteins are separately described, but we note the parallel development that is present in both research fields with three important themes: firstly, combining CG modelling with knowledge-based approaches to predict and…

Volume 23, Issue 6, 01 December 2013, Pp 878-886
Marc Baaden | Siewert J. Marrink

Relating sequence encoded information to form and function of intrinsically disordered proteins

© 2015 Elsevier Ltd. Intrinsically disordered proteins (IDPs) showcase the importance of conformational plasticity and heterogeneity in protein function. We summarize recent advances that connect information encoded in IDP sequences to their conformational properties and functions. We focus on insights obtained through a combination of atomistic simulations and biophysical measurements that are synthesized into a coherent framework using polymer physics theories.

Volume 32, Issue , 01 June 2015, Pp 102-112
Rahul K. Das | Kiersten M. Ruff | Rohit V. Pappu