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- Volume 15, Issue 9, 2008
Protein and Peptide Letters - Volume 15, Issue 9, 2008
Volume 15, Issue 9, 2008
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Editorial
By Ben M. DunnFirst 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, Read More
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Targeting the Plasmepsin 4 Orthologs of Plasmodium sp. with “Double Drug” Inhibitors
Authors: Linda Janka, Jose Clemente, N. Vaiana, A. Sparatore, Sergio Romeo and Ben M. DunnPlasmepsin 4 (PM4) is a digestive vacuole enzyme found in all Plasmodium species examined to date. While P. falciparum has three additional aspartic proteinases in its digestive vacuole in addition to plasmepsin 4, other Plasmodium species have only PM4 in their digestive vacuole. Therefore, PM4 may be a good target for the development of an antimalarial drug. This study presents data obtained with PM4s from se Read More
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Structural and Biochemical Investigation of Heptad Repeat Derived Peptides of Human SARS Corona Virus (hSARS-CoV) Spike Protein+
Authors: Sarmistha Basak, Xiaolei Hao, Andrew Chen, Michel Chretien and Ajoy BasakhSARS-CoV is the causative agent for SARS infection. Its spike glycoprotein (S) is processed by host furin enzyme to produce S1 and S2 fragments, the latter being crucial for fusion with the host membrane. This takes place via formation of a coiled coil 6-helix bundle involving N and Cterminal heptad repeat domains (HR-N and HR-C) of S2. Several fluorescent and non-fluorescent peptides from these domains were synthesized t Read More
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Identification of a Thermo-Regulated Glutamine-Binding Protein from Yersinia pestis
Authors: Monique Cosman, Joseph B. Pesavento, Adam Zemla, Peter T. Beernink, Rod Balhorn and Daniel BarskyHere we present modeling and NMR spectroscopic evidence that the function of a Yersinia pestis pMT1 plasmid protein, designated as orf38, is most likely a glutamine binding protein. The modeling was homology-based at a very low level of sequence identity (∼ 16%) and involved structural comparison of multiple templates, as well as template-substrate interaction analyses. Transferred nuclear Overhauser and saturation tr Read More
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Is Asparagine Deamidation in the Porcine Odorant-Binding Protein Related to the Odor Molecules Binding?
Authors: Gianfranco Mamone and Sabato D'AuriaOdorant-binding proteins are biomolecules belonging to the lipocalin family. Among all the odorant-binding proteins, the porcine odorant-binding protein has been well characterized. This protein is a monomer that is characterized by the presence of the β-barrel structure and of the disulphide bridge. The internal cavity of the β-barrel is the binding site. In this study we have investigated the structural properties of the porcine o Read More
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Pt2L4 Protein, a Homologue to Hev b 5 from Rubber Tree, May Not Be Responsible for the Cross-Reactions to Cassava Show by People Allergic to Latex
More LessPt2L4 is a protein from cassava homologue to Hevb5, a principal allergen from latex. Here we aimed to elucidate immunological relationships between these proteins. Our results revealed that epitopes found in Hev b 5 are not entirely conserved in Pt2L4 which is not recognized by IgE from patients allergic to Hev b 5.
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Structural Refinement of Insecticidal Plant Proteinase Inhibitors from Nicotiana alata
Authors: Horst J. Schirra, Marilyn A. Anderson and David J. CraikOrnamental tobacco (Nicotiana alata) produces a series of 6 kDa proteinase inhibitors belonging to the potato type II inhibitor family. These proteins inhibit trypsin and chymotrypsin, the main digestive enzymes of predatory insects, thus leading to starvation, impaired larval development or death. In this context, the three-dimensional structures of these inhibitors are important for developing novel strategies for pest contr Read More
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Binding Mode of α-Conotoxins to an Acetylcholine Binding Protein Determined by Saturation Transfer Difference NMR
Authors: Jan-Christoph Westermann, Richard J. Clark and David J. CraikThe saturation transfer difference (STD) NMR technique was employed to study the complex of the α-conotoxins Vc1.1 and MII bound to the acetylcholine binding protein (AChBP) from Lymnea stagnalis, a model system of the α7 subunit of the nicotinic acetylcholine receptor. MII was found to be the more potent ligand for AChBP, consistent with data from electrophysiology measurements for the nicotinic acetylcholine Read More
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Predicting Membrane Protein Types by the LLDA Algorithm
Authors: Tong Wang, Jie Yang, Hong-Bin Shen and Kuo-Chen ChouMembrane proteins are generally classified into the following eight types: (1) type I transmembrane, (2) type II, (3) type III, (4) type IV, (5) multipass transmembrane, (6) lipid-chain-anchored membrane, (7) GPI-anchored membrane, and (8) peripheral membrane (K.C. Chou and H.B. Shen: BBRC, 2007, 360: 339-345). Knowing the type of an uncharacterized membrane protein often provides useful clues for finding its biological fun Read More
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Influenza A Virus M1 Protein Structure Probed by In Situ Limited Proteolysis with Bromelain
Influenza A virus matrix M1 protein is membrane associated and plays a crucial role in virus assembly and budding. The N-terminal two thirds of M1 protein was resolved by X-ray crystallography. The overall 3D structure as well as arrangement of the molecule in relation to the viral membrane remains obscure. Now a proteolytic digestion of virions with bromelain was used as an instrument for the in situ assessment of the M1 p Read More
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Elucidation of Structural Requirements of Mastoparan for Mast Cell Activation- Toward the Comprehensive Prediction of Cryptides Acting on Mast Cells
Authors: H. Mukai, Y. Suzuki, Y. Kiso and E. MunekataMastoparan, a toxic peptide from wasp venom, induces various biological functions including histamine release from rat peritoneal mast cells. Here we report that, for the activation of mast cells by mastoparan, at least two positively charged side chains are required on the hydrophilic side of the amphiphilic structure of the peptide. The present results are expected to be utilized for the bioinformatic and comprehensive identificati Read More
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Characterization of the Active Site and a Unique Uncompetitive Inhibitor of the PPM1-Type Protein Phosphatase PPM1D
Protein phosphatase magnesium-dependent 1, delta (PPM1D) is a member of the PPM1 (formerly PP2C) protein phosphatase family, and is induced in response to DNA damage. The overexpression of PPM1D is thought to exert oncogenic effects through the inhibition of tumor suppressor proteins. PPM1D shows high selectivity for the primary sequence in its substrates when compared with other phosphatases, but the mec Read More
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Radar Chart Deviation Analysis of Prion Protein Amino Acid Composition Defines Characteristic Structural Abnormalities of the N-Terminal Octapeptide Tandem Repeat
Authors: Satoru Yokotani, Takeru Nose, Yuji Horiuchi, Ayami Matsushima and Yasuyuki ShimohigashiAnalysis of the amino acid composition of prion protein using a newly developed program for radar-chart deviation analysis has identified an abnormality or irregularity of the N-terminal flexible domain. Aromatic amino acids Trp and His together with Gly are abnormally abounding in this Nterminal domain, in which octapeptide GQPHGGGW is connected four times in tandem. This tetrarepeat structure has been suggested Read More
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TOP-IDP-Scale: A New Amino Acid Scale Measuring Propensity for Intrinsic Disorder
Authors: Andrew Campen, Ryan M. Williams, Celeste J. Brown, Jingwei Meng, Vladimir N. Uversky and A. K. DunkerIntrinsically disordered proteins carry out various biological functions while lacking ordered secondary and/or tertiary structure. In order to find general intrinsic properties of amino acid residues that are responsible for the absence of ordered structure in intrinsically disordered proteins we surveyed 517 amino acid scales. Each of these scales was taken as an independent attribute for the subsequent analysis. For a given att Read More
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Structural Fragments in Protein Model Refinement
Authors: S. M. Hollup, W. R. Taylor and I. JonassenWe survey a method that uses patterns of residue packing in known protein structures to refine structural models. The method can be used to refine models that include only one coordinate point per residue (Cα) and is not dependent on homology. We demonstrate that the method improves both decoy and CASP7 target models.
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Equilibrium Folding of Porcine Insulin Precursor in the Presence of Redox Buffer: Implications for the Common Intermediates Shared by Its Unfolding/ Refolding Processes
Authors: Jie Zhao, Qi-Long Huang, Yue-Hua Tang, Zhan-Yun Guo, Zhi-Song Qiao, Gen-Jun Xu and You-Min FengWe use the procedure established for ‘disulfide stability analysis in redox system’ to investigate the unfolding process of porcine insulin precursor (PIP). Six major unfolding intermediates have been captured, in which four contain two disulfides, two contain one disulfide. Based on the characterization and analysis of the intermediates an unfolding pathway has been proposed, by which the native PIP unfolded through in Read More
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Synthesis and Structural Analysis of 6-Aminobicyclo[2.2.1]heptane-2- carboxylic Acid as a onformationally Constrained γ-Turn Mimic
An efficient asymmetric synthesis of 6-aminobicyclo[2.2.1]heptane-2-carboxylic acid as a novel γ-turn mimic has been achieved. Structural analysis of the γ-amino acid derivative was carried out using 1H NMR spectroscopy and intramolecular hydrogen bonding between side chain amides confirmed the turn structure, which had been predicted by Ab initio computational study.
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Strategies for Recombinant Expression of Small, Highly Disulphide- Bonded, Cationic Antimicrobial Peptides
Authors: A. L. Greenshields, L. C. Knickle, R. Syvitski and S. E. DouglasExpression of two recombinant hepcidin homologues from Atlantic salmon, Salmo salar, characterization of their antimicrobial activity, and partial structural determination of the peptides is described. Expression was attempted in baculovirus and bacterial expression systems and the various purification and refolding methods used to determine the optimal strategy for production of active, correctly refolded hepcidin are reviewed.
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Neutrophil Proteome: Lessons from Different Standpoints
Authors: C. F.M. Morris, M. S. Castro and W. FontesThe present review brings a timeline of some of the major steps given throughout the years towards the development of our knowledge regarding the biology of the neutrophil. The contribution of early articles and their elementary biochemical approach is highlighted. The importance of the development of proteomic techniques is paralleled to the shift in neutrophil research towards high throughput molecular methods. As a l Read More
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Biochemical and Structural Investigations of Bothropstoxin-II, a Myotoxic Asp49 Phospholipase A2 from Bothrops jararacussu Venom
Bothropstoxin-II a calcium-dependent enzyme from Bothrops jararacussu venom causes tissue damage and several haemostatic disorders including platelet aggregation. In order to elucidate the structural determinants of its multiple pharmacological activities, we have studied the effects of suramin on Bothropstoxin-II and present details concerning the mode of binding.
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Volumes & issues
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Volume 32 (2025)
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Volume 31 (2024)
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Volume 30 (2023)
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Volume 29 (2022)
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Volume 28 (2021)
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Volume 27 (2020)
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Volume 26 (2019)
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Volume 25 (2018)
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Volume 24 (2017)
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Volume 23 (2016)
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Volume 22 (2015)
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Volume 21 (2014)
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Volume 20 (2013)
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Volume 19 (2012)
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Volume 18 (2011)
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Volume 17 (2010)
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Volume 16 (2009)
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Volume 15 (2008)
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Volume 14 (2007)
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Volume 13 (2006)
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Volume 12 (2005)
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Volume 11 (2004)
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Volume 10 (2003)
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Volume 9 (2002)
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Volume 8 (2001)
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