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 17 leading titles in life sciences and adjacent fields.

Current Opinion in Structural Biology

5-Year Impact Factor: 9.113
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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Linking folding and binding

Many cellular proteins are intrinsically disordered and undergo folding, in whole or in part, upon binding to their physiological targets. The past few years have seen an exponential increase in papers describing characterization of intrinsically disordered proteins, both free and bound to targets. Although NMR spectroscopy remains the favored tool, a number of new biophysical techniques are proving exceptionally useful in defining the limits of the conformational ensembles. Advances have been…

Volume 19, Issue 1, 01 February 2009, Pp 31-38
Peter E. Wright | H. Jane Dyson

Long-timescale molecular dynamics simulations of protein structure and function

Molecular dynamics simulations allow for atomic-level characterization of biomolecular processes such as the conformational transitions associated with protein function. The computational demands of such simulations, however, have historically prevented them from reaching the microsecond and greater timescales on which these events often occur. Recent advances in algorithms, software, and computer hardware have made microsecond-timescale simulations with tens of thousands of atoms practical,…

Volume 19, Issue 2, 01 April 2009, Pp 120-127
John L. Klepeis | Kresten Lindorff-Larsen | Ron O. Dror | David Elliott Shaw

The structures of quadruplex nucleic acids and their drug complexes

Quadruplex nucleic acids are four-stranded structures formed from short tracts of G-rich sequence associating together. Their formation from eukaryotic telomeric DNA sequences is well established, at least in vitro, and has more recently been the focus of attention as novel anticancer targets since their formation inhibits the telomerase complex from maintaining telomere length in cancer cells. Structural studies have revealed a diversity of topologies for telomeric quadruplexes, which are…

Volume 19, Issue 3, 01 June 2009, Pp 239-250
Stephen Neidle

SF1 and SF2 helicases: Family matters

Helicases of the superfamily (SF) 1 and 2 are involved in virtually all aspects of RNA and DNA metabolism. SF1 and SF2 helicases share a catalytic core with high structural similarity, but different enzymes even within each SF perform a wide spectrum of distinct functions on diverse substrates. To rationalize similarities and differences between these helicases, we outline a classification based on protein families that are characterized by typical sequence, structural, and mechanistic…

Volume 20, Issue 3, 01 June 2010, Pp 313-324
Margaret E. Fairman-Williams | Ulf Peter Guenther | Eckhard Jankowsky

Sialic acids as regulators of molecular and cellular interactions

The wide occurrence of sialic acids (Sia) in various chemical forms linked as monomers or polymers in an outstanding position in a multitude of complex carbohydrates of animals and microorganisms renders them as most versatile function modulators in cell biology and pathology. A survey is presented of recent advances in the study of the influences that Sias have as bulky hydrophilic and electronegatively charged monosaccharides on animal cells and on their interaction with microorganisms. Some…

Volume 19, Issue 5, 01 October 2009, Pp 507-514
Roland Schauer

Poly(dA:dT) tracts: major determinants of nucleosome organization

Homopolymeric stretches of deoxyadenosine nucleotides (A's) on one strand of double-stranded DNA, referred to as poly(dA:dT) tracts or A-tracts, are overabundant in eukaryotic genomes. They have unusual structural, dynamic, and mechanical properties, and may resist sharp bending. Such unusual material properties, together with their overabundance in eukaryotes, raised the possibility that poly(dA:dT) tracts might function in eukaryotes to influence the organization of nucleosomes at many…

Volume 19, Issue 1, 01 February 2009, Pp 65-71
Eran Segal | Jonathan Widom

Biophysical characterization of intrinsically disordered proteins

The challenges associated with the structural characterization of disordered proteins have resulted in the application of a host of biophysical methods to such systems. NMR spectroscopy is perhaps the most readily suited technique for providing high-resolution structural information on disordered protein states in solution. Optical methods, solid state NMR, ESR and X-ray scattering can also provide valuable information regarding the ensemble of conformations sampled by disordered states.…

Volume 19, Issue 1, 01 February 2009, Pp 23-30
David Eliezer

Stability effects of mutations and protein evolvability

The past several years have seen novel insights at the interface of protein biophysics and evolution. The accepted paradigm that proteins can tolerate nearly any amino acid substitution has been replaced by the view that the deleterious effects of mutations, and especially their tendency to undermine the thermodynamic and kinetic stability of protein, is a major constraint on protein evolvability-the ability of proteins to acquire changes in sequence and function. We summarize recent findings…

Volume 19, Issue 5, 01 October 2009, Pp 596-604
Nobuhiko Tokuriki | Dan S. Tawfik

Advances and pitfalls of protein structural alignment

Structure comparison opens a window into the distant past of protein evolution, which has been unreachable by sequence comparison alone. With 55 000 entries in the Protein Data Bank and about 500 new structures added each week, automated processing, comparison, and classification are necessary. A variety of methods use different representations, scoring functions, and optimization algorithms, and they generate contradictory results even for moderately distant structures. Sequence mutations,…

Volume 19, Issue 3, 01 June 2009, Pp 341-348
Hitomi Hasegawa | Liisa Holm

Models of macromolecular crowding effects and the need for quantitative comparisons with experiment

In recent years significant effort has been devoted to exploring the potential effects of macromolecular crowding on protein folding and association phenomena. Theoretical calculations and molecular simulations have, in particular, been exploited to describe aspects of protein behavior in crowded and confined conditions and many aspects of the simulated behavior have reflected, at least at a qualitative level, the behavior observed in experiments. One major and immediate challenge for the…

Volume 20, Issue 2, 01 April 2010, Pp 196-206
Adrian H. Elcock

Force and function: probing proteins with AFM-based force spectroscopy

Forces play a pivotal role in life, and the response of live systems to forces requires molecules and molecular interactions with adequate properties to counteract both in a passive and also, if needed, in an active, dynamic manner. However, at the level of individual molecules these forces are so minute, that the development of sophisticated experiments to measure and control them was required. With the maturation of these techniques, particularly the AFM-based single-molecule force…

Volume 19, Issue 5, 01 October 2009, Pp 605-614
Elias M. Puchner | Hermann E. Gaub

Convergence and combination of methods in protein-protein docking

The analysis of results from Critical Assessment of Predicted Interactions (CAPRI), the first community-wide experiment devoted to protein docking, shows that all successful methods consist of multiple stages. The methods belong to three classes: global methods based on fast Fourier transforms (FFTs) or geometric matching, medium-range Monte Carlo methods, and the restraint-guided High Ambiguity Driven biomolecular DOCKing (HADDOCK) program. Although these classes of methods require very…

Volume 19, Issue 2, 01 April 2009, Pp 164-170
Sándor Vajda | Dima Kozakov

Mass spectrometry in the analysis of N-linked and O-linked glycans

Mass spectrometry (MS) continues to play a vital role in defining the structures of N-glycans and O-glycans in glycoproteins via glycomic and glycoproteomic methodologies. The former seeks to define the total N-glycan and/or O-glycan repertoire in a biological sample whilst the latter is concerned with the analysis of glycopeptides. Recent technical developments have included improvements in tandem mass spectrometry (MS/MS and MSn) sequencing methodologies, more sensitive methods for analysing…

Volume 19, Issue 5, 01 October 2009, Pp 498-506
Simon J. North | Paul G. Hitchen | Stuart M. Haslam | Anne E. Dell

Structure and function of Na+-symporters with inverted repeats

Symporters are membrane proteins that couple energy stored in electrochemical potential gradients to drive the cotransport of molecules and ions into cells. Traditionally, proteins are classified into gene families based on sequence homology and functional properties, for example the sodium glucose (SLC5 or Sodium Solute Symporter Family, SSS or SSF) and GABA (SLC6 or Neurotransmitter Sodium Symporter Family, NSS or SNF) symporter families [1-4]. Recently, it has been established that four…

Volume 19, Issue 4, 01 August 2009, Pp 425-432
Jeff Abramson | Ernest M. Wright

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
Péter Tompa

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
Madan Madan Babu | Robin Van der Lee | Natalia Sanchez de Groot | Jörg A. Gsponer

Molecular dynamics simulations of membrane channels and transporters

Membrane transport constitutes one of the most fundamental processes in all living cells with proteins as major players. Proteins as channels provide highly selective diffusive pathways gated by environmental factors, and as transporters furnish directed, energetically uphill transport consuming energy. X-ray crystallography of channels and transporters furnishes a rapidly growing number of atomic resolution structures, permitting molecular dynamics (MD) simulations to reveal the physical…

Volume 19, Issue 2, 01 April 2009, Pp 128-137
Fatemeh Khalili-Araghi | James Conrad Gumbart | Pochao Wen | Marcos Sotomayor | Emad Tajkhorshid | Klaus J. Schulten

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

Glycoprotein folding, quality control and ER-associated degradation

Nascent N-linked glycoproteins possess a large oligosaccharide precursor, Glc3Man9GlcNAc2, which is later sequentially trimmed. Recent studies help understand the code displayed by each structure produced by this trimming and its decoding by lectins. The calnexin folding cycle targets only monoglucosylated oligosaccharides. N-glycans of misfolded glycoproteins are then more extensively trimmed than once thought, being targeted for degradation by removal of three or four mannose residues. A high…

Volume 19, Issue 5, 01 October 2009, Pp 515-523
Gerardo Z. Lederkremer

Gangliosides in cell recognition and membrane protein regulation

Gangliosides, sialic acid-bearing glycosphingolipids, are expressed on all vertebrate cells, and are the major glycans on nerve cells. They are anchored to the plasma membrane through their ceramide lipids with their varied glycans extending into the extracellular space. Through sugar-specific interactions with glycan-binding proteins on apposing cells, gangliosides function as receptors in cell-cell recognition, regulating natural killer cell cytotoxicity via Siglec-7, myelin-axon interactions…

Volume 19, Issue 5, 01 October 2009, Pp 549-557
P. H. López | Ronald L. Schnaar

Structural biology in fragment-based drug design

Fragment-based ligand screening is now established as an emerging paradigm for drug discovery. Here we examine the recent literature looking at how structural biology has been used in a variety of successful fragment-screening applications. We argue that the determination of experimental binding modes has proved to be one of the mainstays of successful fragment-based approaches and that this reflects the difficulty in optimising a fragment to a lead molecule in the absence of structural…

Volume 20, Issue 4, 01 August 2010, Pp 497-507
Christopher W. Murray | Tom Leon Blundell

Protein structure prediction: when is it useful?

Computationally predicted three-dimensional structure of protein molecules has demonstrated the usefulness in many areas of biomedicine, ranging from approximate family assignments to precise drug screening. For nearly 40 years, however, the accuracy of the predicted models has been dictated by the availability of close structural templates. Progress has recently been achieved in refining low-resolution models closer to the native ones; this has been made possible by combining knowledge-based…

Volume 19, Issue 2, 01 April 2009, Pp 145-155
Yang Zhang

Nonribosomal peptide synthetases: Structures and dynamics

Nonribosomal peptide synthetases (NRPSs) are large multimodular biocatalysts that utilize complex regiospecific and stereospecific reactions to assemble structurally and functionally diverse peptides that have important medicinal applications. During this ribosome-independent peptide synthesis, catalytic domains of NRPS select, activate or modify the covalently tethered reaction intermediates to control the iterative chain elongation process and product release. Recent advances in structural…

Volume 20, Issue 2, 01 April 2010, Pp 234-240
Matthias Strieker | Alan Tanović | Mohamed A. Màrahiel

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 Lowell Mobley | Michael R. Shirts | Richard W. Dixon | Kim M. Branson | Vijay S. Pande

Engineering G protein-coupled receptors to facilitate their structure determination

Over the last two years, 10 new high-resolution structures of G protein-coupled receptors (GPCRs), either with antagonist bound or in an active-like state, have been solved. Whilst the structures of bovine opsin and squid rhodopsin were determined using protein purified from native sources, a rhodopsin mutant structure, the structures of the β1 and β2 adrenergic receptors and the adenosine A2a receptor were determined from engineered protein heterologously expressed in either insect or…

Volume 19, Issue 4, 01 August 2009, Pp 386-395
Christopher Tate | Gebhard FX X Schertler