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.

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Mechanisms and principles of N-linked protein glycosylation

N-linked glycosylation, a protein modification system present in all domains of life, is characterized by a high structural diversity of N-linked glycans found among different species and by a large number of proteins that are glycosylated. Based on structural, functional, and phylogenetic approaches, this review discusses the highly conserved processes that are at the basis of this unique general protein modification system. © 2011 Elsevier Ltd.

Volume 21, Issue 5, 01 October 2011, Pp 576-582
Flavio Schwarz | Markus Aebi

Intrinsically disordered proteins: Regulation and disease

Intrinsically disordered proteins (IDPs) are enriched in signaling and regulatory functions because disordered segments permit interaction with several proteins and hence the re-use of the same protein in multiple pathways. Understanding IDP regulation is important because altered expression of IDPs is associated with many diseases. Recent studies show that IDPs are tightly regulated and that dosage-sensitive genes encode proteins with disordered segments. The tight regulation of IDPs may…

Volume 21, Issue 3, 01 June 2011, Pp 432-440
M. Madan Babu | Robin van der Lee | Natalia Sanchez de Groot | Jörg Gsponer

Unstructural biology coming of age

It is now generally accepted that many proteins or protein domains (intrinsically disordered proteins, IDPs) lack a well-defined tertiary structure under functional conditions. Due to recent concerted activity, a critical transition in this field is gaining momentum, in which qualitative observations are turned into quantitative structural models of IDPs. Here, it is suggested that the transition is set up by the synergy of: (i) more advanced bioinformatic tools for the prediction of disorder…

Volume 21, Issue 3, 01 June 2011, Pp 419-425
Peter Tompa

Alchemical free energy methods for drug discovery: Progress and challenges

Improved rational drug design methods are needed to lower the cost and increase the success rate of drug discovery and development. Alchemical binding free energy calculations, one potential tool for rational design, have progressed rapidly over the past decade, but still fall short of providing robust tools for pharmaceutical engineering. Recent studies, especially on model receptor systems, have clarified many of the challenges that must be overcome for robust predictions of binding affinity…

Volume 21, Issue 2, 01 April 2011, Pp 150-160
John D. Chodera | David L. Mobley | Michael R. Shirts | Richard W. Dixon | Kim Branson | Vijay S. Pande

Mass spectrometry: Come of age for structural and dynamical biology

Over the past two decades, mass spectrometry (MS) has emerged as a bone fide approach for structural biology. MS can inform on all levels of protein organization, and enables quantitative assessments of their intrinsic dynamics. The key advantages of MS are that it is a sensitive, high-resolution separation technique with wide applicability, and thereby allows the interrogation of transient protein assemblies in the context of complex mixtures. Here we describe how molecular-level information…

Volume 21, Issue 5, 01 October 2011, Pp 641-649
Justin L P Benesch | Brandon T. Ruotolo

Protein dynamics and allostery: An NMR view

Allostery, the process by which distant sites within a protein system are energetically coupled, is an efficient and ubiquitous mechanism for activity regulation. A purely mechanical view of allostery invoking only structural changes has developed over the decades as the classical view of the phenomenon. However, a fast growing list of examples illustrate the intimate link between internal motions over a wide range of time scales and function in protein-ligand interactions. Proteins respond to…

Volume 21, Issue 1, 01 February 2011, Pp 62-67
Shiou Ru Tzeng | Charalampos G. Kalodimos

Constructing ensembles for intrinsically disordered proteins

The relatively flat energy landscapes associated with intrinsically disordered proteins makes modeling these systems especially problematic. A comprehensive model for these proteins requires one to build an ensemble consisting of a finite collection of structures, and their corresponding relative stabilities, which adequately capture the range of accessible states of the protein. In this regard, methods that use computational techniques to interpret experimental data in terms of such ensembles…

Volume 21, Issue 3, 01 June 2011, Pp 426-431
Charles K. Fisher | Collin M. Stultz

Structural insights into agonist-induced activation of G-protein-coupled receptors

Recent years have seen tremendous breakthroughs in structure determination of G-protein-coupled receptors (GPCRs). In 2011, two agonist-bound active-state structures of rhodopsin have been published. Together with structures of several rhodopsin activation intermediates and a wealth of biochemical and spectroscopic information, they provide a unique structural framework on which to understand GPCR activation. Here we use this framework to compare the recent crystal structures of the…

Volume 21, Issue 4, 01 August 2011, Pp 541-551
Xavier Deupi | Jörg Standfuss

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

Nanobody stabilization of G protein-coupled receptor conformational states

Remarkable progress has been made in the field of G protein-coupled receptor (GPCR) structural biology during the past four years. Several obstacles to generating diffraction quality crystals of GPCRs have been overcome by combining innovative methods ranging from protein engineering to lipid-based screens and microdiffraction technology. The initial GPCR structures represent energetically stable inactive-state conformations. However, GPCRs signal through different G protein isoforms or G…

Volume 21, Issue 4, 01 August 2011, Pp 567-572
Jan Steyaert | Brian K. Kobilka

Protein binding specificity versus promiscuity

Interactions between macromolecules in general, and between proteins in particular, are essential for any life process. Examples include transfer of information, inhibition or activation of function, molecular recognition as in the immune system, assembly of macromolecular structures and molecular machines, and more. Proteins interact with affinities ranging from millimolar to femtomolar and, because affinity determines the concentration required to obtain 50% binding, the amount of different…

Volume 21, Issue 1, 01 February 2011, Pp 50-61
Gideon Schreiber | Amy E. Keating

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

Evolution and disorder

The evolution of disordered proteins or regions of proteins differs from that of ordered proteins because of the differences in their sequence composition, intramolecular contacts, and function. Recent assessments of disordered protein evolution at the sequence, structural, and functional levels support this hypothesis. Disordered proteins have a different pattern of accepted point mutations, exhibit higher rates of insertions and deletions, and generally, but not always, evolve more rapidly…

Volume 21, Issue 3, 01 June 2011, Pp 441-446
Celeste J. Brown | Audra K. Johnson | A. Keith Dunker | Gary W. Daughdrill

Structural regulation of cullin-RING ubiquitin ligase complexes

Cullin-RING ligases (CRLs) compose the largest class of E3 ubiquitin ligases. CRLs are modular, multisubunit enzymes, comprising interchangeable substrate receptors dedicated to particular Cullin-RING catalytic cores. Recent structural studies have revealed numerous ways in which CRL E3 ligase activities are controlled, including multimodal E3 ligase activation by covalent attachment of the ubiquitin-like protein NEDD8, inhibition of CRL assembly/activity by CAND1, and several mechanisms of…

Volume 21, Issue 2, 01 April 2011, Pp 257-264
David M. Duda | Daniel C. Scott | Matthew F. Calabrese | Erik S. Zimmerman | Ning Zheng | Brenda A. Schulman

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

Coarse-grained models for protein aggregation

The aggregation of soluble proteins into fibrillar species is a complex process that spans many lengths and time scales, and that involves the formation of numerous on-pathway and off-pathway intermediate species. Despite this complexity, several elements underlying the aggregation process appear to be universal. The kinetics typically follows a nucleation-growth process, and proteins with very different sequences aggregate to form similar fibril structures, populating intermediates with…

Volume 21, Issue 2, 01 April 2011, Pp 209-220
Chun Wu | Joan Emma Shea

Strategy and success for the directed evolution of enzymes

Directed evolution is widely used to improve enzymes, particularly for industrial biocatalytic processes. Molecular biology advances present many new strategies for directed evolution. Commonly used techniques have led to many successful examples of enzyme improvement, yet there is still a need to improve both the efficiency and capability of directed evolution. Recent strategies aimed at making directed evolution faster and more efficient take better advantage of available structural and…

Volume 21, Issue 4, 01 August 2011, Pp 473-480
Paul A. Dalby

Taming the complexity of protein folding

Protein folding is an important problem in structural biology with significant medical implications, particularly for misfolding disorders like Alzheimer's disease. Solving the folding problem will ultimately require a combination of theory and experiment, with theoretical models providing a comprehensive view of folding and experiments grounding these models in reality. Here we review progress towards this goal over the past decade, with an emphasis on recent theoretical advances that are…

Volume 21, Issue 1, 01 February 2011, Pp 4-11
Gregory R. Bowman | Vincent A. Voelz | Vijay S. Pande

Structure-based systems biology for analyzing off-target binding

Here off-target binding implies the binding of a small molecule of therapeutic interest to a protein target other than the primary target for which it was intended. Increasingly such off-targeting appears to be the norm rather than the exception, rational drug design notwithstanding, and can lead to detrimental side-effects, or opportunities to reposition a therapeutic agent to treat a different condition. Not surprisingly, there is significant interest in determining a priori what off-targets…

Volume 21, Issue 2, 01 April 2011, Pp 189-199
Lei Xie | Li Xie | Philip E. Bourne

Protein folding in the cell: Challenges and progress

It is hard to imagine a more extreme contrast than that between the dilute solutions used for in vitro studies of protein folding and the crowded, compartmentalized, sticky, spatially inhomogeneous interior of a cell. This review highlights recent research exploring protein folding in the cell with a focus on issues that are generally not relevant to in vitro studies of protein folding, such as macromolecular crowding, hindered diffusion, cotranslational folding, molecular chaperones, and…

Volume 21, Issue 1, 01 February 2011, Pp 32-41
Anne Gershenson | Lila M. Gierasch

Lipidic cubic phase technologies for membrane protein structural studies

Lipidic cubic phase (LCP) is a membrane-mimetic matrix suitable for stabilization and crystallization of membrane proteins in lipidic environment. LCP technologies, however, have not been fully embraced by the membrane protein structural biology community, primarily because of the difficulties associated with handling viscous materials. Recent developments of pre-crystallization assays and improvements in crystal imaging, successes in obtaining high resolution structures of G protein-coupled…

Volume 21, Issue 4, 01 August 2011, Pp 559-566
Vadim Cherezov

Near-atomic resolution reconstructions of icosahedral viruses from electron cryo-microscopy

Nine different near-atomic resolution structures of icosahedral viruses, determined by electron cryo-microscopy and published between early 2008 and late 2010, fulfil predictions made 15 years ago that single-particle cryo-EM techniques could visualize molecular detail at 3-4. Å resolution. This review summarizes technical developments, both in instrumentation and in computation, that have led to the new structures, which advance our understanding of virus assembly and cell entry. © 2011…

Volume 21, Issue 2, 01 April 2011, Pp 265-273
Nikolaus Grigorieff | Stephen C. Harrison

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

Uncovering the intimate relationship between lipids, cholesterol and GPCR activation

The membrane bilayer has a significant influence over the proteins embedded within it. G protein-coupled receptors (GPCRs) form a large group of membrane proteins with a vast array of critical functions, and direct and indirect interactions with the bilayer are thought to control various essential aspects of receptor function. The presence of cholesterol, in particular, has been the focus of a number of recent studies, with varying receptor-dependent effects reported. However, the possibility…

Volume 21, Issue 6, 01 December 2011, Pp 802-807
Joanne Oates | Anthony Watts