Editorial

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First a few notes on the operation of the journal: We have just made the decision to change to 12 issues per year starting in 2009, up from 10 issues this year. This is due to the very heavy manuscript flow that we have been experiencing in 2008. In addition, the larger size and two column format, initiated in 2005 with volume 12, have been well received. Improvements have also been made with respect to reproduction of figures, although this will always be dependent upon getting high quality files from the authors. We have seen a growth in the Impact Factor and expect this to continue. I want to express my appreciation to Miss Sarwat Aziz Abbasi of the publisher's office for all her help with all matters involving the journal.

We are very grateful to the members of the Editorial Advisory Board (EAB) for Protein and Peptide Letters for their efforts over the years to review manuscripts, to submit their own work, to recommend referees, and to critique the operation of all aspects of the journal. Over the past 15 years we have added new members to the EAB, thanked retiring members, and added new Regional Editors to help with the increasing manuscript flow we have experienced. While we are actively soliciting new individuals at this time, we are always open to self-nomination from interested readers of the journal.

In this issue, we inaugurate a special feature that we hope will prove to be valuable for all readers. This issue features contributions from members of the EAB. This should help other scientists to identify with some EAB member when submitting their work to PPL. By identifying an EAB member who works in the area that you do to oversee the peer review process, you can insure that your manuscript will get a fair analysis by an expert in the field. For the same reason, to insure fair peer review, we ask that all submissions be accompanied by a list of four or more potential referees.

The contributions in this issue were subjected to the same peer review process as all manuscripts and all went through a round of revision. The contributions cover a wide range of protein and peptide science. The first five papers loosely deal with studies of binding interactions between proteins and other molecules. Dunn and colleagues report on of a series of statine-based inhibitors binding to enzymes of the plasmepsin family as part of a study on potential antimalarial drugs. Ajoy Basak and coworkers report on the properties of heptad repeats from a fragment of the spike surface glycoprotein of the SARS virus. Monique Cosman, Daniel Barsky and their colleagues discuss the function of a specific Yersinia pestis gene product and conclude that it is most likely a glutamine binding protein. Odorant binding proteins are β-barrel proteins with the cavity inside the barrel serving as the binding site. Mamone and D'Auria report on the effects of deamination of a porcine odorant binding protein on its function. Claudia Regina Batista de Souza and her colleagues examine the possible cross reaction between sensitivity to latex and to proteins from the cassava plant.

The next ten papers deal with structural analysis and prediction. David Craik's lab has contributed two papers to this issue: in the first, Schirra, Anderson, and Craik report on the structural refinement of NMR analysis of protease inhibitors from the tobacco plant; in the second paper, Westermann, Clark, and Craik use NMR to study the binding mode of α-conotoxins to an acetylcholine binding protein. Predicting membrane protein types is a new process of great importance in this post-genomic world. Kuo-Chen Chou and his colleagues apply a new program, called Local Linear Discriminant Analysis, to this job.

The matrix protein M1 plays an important role in influenza virus growth and Kordyukova and her colleagues have used bromelain digestion to obtain information on the properties of M1. Identifying peptide segments hidden within protein sequences, which are termed cryptides, is described by Mukai and his colleagues in their discussion of the effects of several peptides on histamine release from mast cells. Kazuyasu Sakaguchi and co-authors discuss a subfamily of the protein phosphatases, the magnesium dependent phosphatases and use bioinformatic methods to identify active site residues and to analyze substrate specificity. The prion protein has an N-terminus that includes four repeats of the peptide sequence Gly-Gln- Phe-His-Gly-Gly-Gly-Trp. Shimohigashi and his colleagues analyze the amino acid composition of different parts of the prion protein using the Radar Chart method. An exciting new area of protein research involves intrinsically disordered proteins. Vladimir Uversky, Keith Dunker and their associates discuss the use of the TOP-IDP-Scale, a new prediction tool for measuring the propensity for intrinsic disorder. Willy Taylor and his colleagues Hollup and Jonassen describe the use of protein fragments in protein modeling and structure prediction. You-Ming Feng and his co-workers report on studies of the equilibrium folding of the proinsulin precursor protein. B. Moon Kim and his colleagues describe the synthesis of a conformationally constrained γ-turn mimic.......

Document Type: Research Article

DOI: http://dx.doi.org/10.2174/092986608785849317

Publication date: September 1, 2008

More about this publication?
  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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