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: 6.965
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.

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.

Subscribe to RSS Sciverse Scopus

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

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

Coarse-grained molecular simulations of large biomolecules

Recently, we saw a dramatic increase in the number of researches that rely on coarse-grained (CG) simulations for large biomolecules. Here, first, we briefly describe recently developed and used CG models for proteins and nucleic acids. Balance between structure-based and physico-chemical terms is a key issue. We also discuss the multiscale algorithms used to derive CG parameters. Next, we comment on the dynamics used in CG simulations with an emphasis on the importance of hydrodynamic…

Volume 22, Issue 2, 01 April 2012, Pp 130-137
Shoji Takada

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

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

Atomistic molecular simulations of protein folding

Theory and experiment have provided answers to many of the fundamental questions of protein folding; a remaining challenge is an accurate, high-resolution picture of folding mechanism. Atomistic molecular simulations with explicit solvent are the most promising method for providing this information, by accounting more directly for the physical interactions that stabilize proteins. Although simulations of folding with such force fields are extremely challenging, they have become feasible as a…

Volume 22, Issue 1, 01 February 2012, Pp 52-61
Robert B. Best

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

Directed enzyme evolution: Beyond the low-hanging fruit

The field of directed evolution has progressed to the point where it is feasible to engineer enzymes for unnatural substrates and reactions with catalytic efficiencies and regio-specificity or stereo-specificity that rival those of natural enzymes. Here, we describe the conceptual and methodological advances that have enabled this progress. We address methodologies based on small libraries enriched with improved variants and carrying compensatory stabilizing mutations. Such libraries can be…

Volume 22, Issue 4, 01 August 2012, Pp 406-412
Moshe Goldsmith | Dan S. Tawfik

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

Recent structures, evolution and mechanisms of glycosyltransferases

Cellular glycome assembly requires the coordinated action of a large number of glycosyltransferases that catalyse the transfer of a sugar residue from a donor to specific acceptor molecules. This enzyme family is very ancient, encompassing all three domains of life. There has been considerable recent progress in structural glycobiology with the determination of crystal structures of several important glycosyltransferase members, showing novel folds and variations around a common α/β scaffold.…

Volume 22, Issue 5, 01 October 2012, Pp 540-549
Christelle Breton | Sylvie Fournel-Gigleux | Monica M. Palcic

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

Iron-sulphur clusters in nucleic acid processing enzymes

Several unexpected reports of iron-sulphur clusters in nucleic acid binding proteins have recently appeared in the literature. Once thought to be relatively rare in these systems, iron-sulphur clusters are now known to be essential components of diverse nucleic acid processing machinery including glycosylases, primases, helicases, nucleases, transcription factors, RNA polymerases and RNA methyltransferases. In many cases, the function of the cluster is poorly understood and crystal structures…

Volume 22, Issue 1, 01 February 2012, Pp 94-100
Malcolm F. White | Mark S. Dillingham

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

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

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

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

Time-resolved structural studies at synchrotrons and X-ray free electron lasers: Opportunities and challenges

X-ray free electron lasers (XFELs) are potentially revolutionary X-ray sources because of their very short pulse duration, extreme peak brilliance and high spatial coherence, features that distinguish them from today's synchrotron sources. We review recent time-resolved Laue diffraction and time-resolved wide angle X-ray scattering (WAXS) studies at synchrotron sources, and initial static studies at XFELs. XFELs have the potential to transform the field of time-resolved structural biology, yet…

Volume 22, Issue 5, 01 October 2012, Pp 651-659
Richard Neutze | Keith Moffat

How, when and why proteins collapse: The relation to folding

Unfolded proteins under strongly denaturing conditions are highly expanded. However, when the conditions are more close to native, an unfolded protein may collapse to a compact globular structure distinct from the folded state. This transition is akin to the coil-globule transition of homopolymers. Single-molecule FRET experiments have been particularly conducive in revealing the collapsed state under conditions of coexistence with the folded state. The collapse can be even more readily…

Volume 22, Issue 1, 01 February 2012, Pp 14-20
Gilad Haran

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

Motif switches: Decision-making in cell regulation

Tight regulation of gene products from transcription to protein degradation is required for reliable and robust control of eukaryotic cell physiology. Many of the mechanisms directing cell regulation rely on proteins detecting the state of the cell through context-dependent, tuneable interactions. These interactions underlie the ability of proteins to make decisions by combining regulatory information encoded in a protein's expression level, localisation and modification state. This raises the…

Volume 22, Issue 3, 01 June 2012, Pp 378-385
Kim Van Roey | Toby J. Gibson | Norman E. Davey

Micro-crystallography comes of age

The latest revolution in macromolecular crystallography was incited by the development of dedicated, user friendly, micro-crystallography beam lines. Brilliant X-ray beams of diameter 20. μm or less, now available at most synchrotron sources, enable structure determination from samples that previously were inaccessible. Relative to traditional crystallography, crystals with one or more small dimensions have diffraction patterns with vastly improved signal-to-noise when recorded with an…

Volume 22, Issue 5, 01 October 2012, Pp 602-612
Janet L. Smith | Robert F. Fischetti | Masaki Yamamoto

How SNARE molecules mediate membrane fusion: Recent insights from molecular simulations

SNARE molecules are the core constituents of the protein machinery that facilitate fusion of synaptic vesicles with the presynaptic plasma membrane, resulting in the release of neurotransmitter. On a molecular level, SNARE complexes seem to play a quite versatile and involved role during all stages of fusion. In addition to merely triggering fusion by forcing the opposing membranes into close proximity, SNARE complexes are now seen to also overcome subsequent fusion barriers and to actively…

Volume 22, Issue 2, 01 April 2012, Pp 187-196
Herre Jelger Risselada | Helmut Grubmüller

Dynamics and mechanisms of coupled protein folding and binding reactions

Protein folding coupled to binding of a specific ligand is frequently observed in biological processes. In recent years numerous studies have addressed the structural properties of the unfolded proteins in the absence of their ligands. Surprisingly few time-resolved investigations on coupled folding and binding reactions have been published up to date and the dynamics and kinetic mechanisms of these processes are still only poorly understood. Especially, it is still unsolved for most systems…

Volume 22, Issue 1, 01 February 2012, Pp 21-29
Thomas Kiefhaber | Annett Bachmann | Kristine Steen Jensen