Journal of Peptide Science

Cover image for Vol. 16 Issue 10

Special Issue: Probing Protein Function through Chemistry

October 2010

Volume 16, Issue 10

Pages 513–600

  1. Editorials

    1. Top of page
    2. Editorials
    3. Reviews
    4. Research Articles
    5. Rapid Communications
    6. Research Articles
    1. Chemical protein synthesis (page 513)

      Paul Alewood, Martin Engelhard and Stephen B. H. Kent

      Version of Record online: 16 SEP 2010 | DOI: 10.1002/psc.1291

  2. Reviews

    1. Top of page
    2. Editorials
    3. Reviews
    4. Research Articles
    5. Rapid Communications
    6. Research Articles
    1. Probing protein function by chemical modification (pages 514–523)

      Yao-Wen Wu and Roger S. Goody

      Version of Record online: 2 SEP 2010 | DOI: 10.1002/psc.1287

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      Labeling proteins using synthetic probes plays an important role in modern biological research at the molecular, cellular and whole organ or animal levels. Recent advances in chemistry and in the combination of chemical and molecular biological approaches have led to significant advances in this field, which are reviewed here.

    2. Accessing posttranslationally modified proteins through thiol positioning (pages 524–529)

      K. S. Ajish Kumar and Ashraf Brik

      Version of Record online: 20 APR 2010 | DOI: 10.1002/psc.1229

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      New ligation methods are presented which allow the total chemical synthesis of posttranslationally modified proteins. The success of these ligation strategies revolved around positioning of a sufhydryl functionality at a suitable position in a peptide to capture a thioester peptide for an amide bond formation.

    3. Chemical tools in chromatin research (pages 530–537)

      Dirk Schwarzer

      Version of Record online: 31 MAR 2010 | DOI: 10.1002/psc.1226

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      Chromatin is the complex of DNA and histone proteins that packages the genome into the limited space of cellular nuclei and regulates the activity of encoded genes. The regulatory processes involve a complex crosstalk between posttranslational histone modifications and chromatin structure which can be studied with sophisticated chemical tools. This review provides an overview of these tools with emphasis on classical and current examples of their applications.

    4. Evolutionary mechanism as a template for protein engineering (pages 538–544)

      Simone Eisenbeis and Birte Höcker

      Version of Record online: 14 MAY 2010 | DOI: 10.1002/psc.1233

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      Many techniques used in protein engineering are successfully mimicking evolutionary processes. First the fundamental evolutionary mechanisms are introduced with a focus on duplication and fusion, recombination, and circular permutation. Then the influence of these mechanisms on protein engineering experiments are discussed.

  3. Research Articles

    1. Top of page
    2. Editorials
    3. Reviews
    4. Research Articles
    5. Rapid Communications
    6. Research Articles
    1. Synthesis and comparative properties of two amide-generating resin linkers for use in solid phase peptide synthesis (pages 545–550)

      Fang-Kun Deng, Kalyaneswar Mandal, Sam Luisier and Stephen B. H. Kent

      Version of Record online: 7 SEP 2010 | DOI: 10.1002/psc.1279

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      We have optimized the preparation of two amide-generating linkers for use in stepwise solid phase peptide synthesis. In combination with aminomethyl-resin prepared directly from polystyrene resin, these linkers serve as alternatives to MBHA-resin for peptide amide synthesis.

    2. Benzhydrylamine linker grafting: a strategy for the improved synthesis of C-terminal peptide amides (pages 551–557)

      Dianne Alewood, Gene Hopping, Andreas Brust, Robert C. Reid and Paul F. Alewood

      Version of Record online: 15 JUN 2010 | DOI: 10.1002/psc.1248

      Thumbnail image of graphical abstract

      Benzhydrylamine enzhydrylamine linkers (a/b) were grafted onto high-performing Phe-PAM resins for Boc solid phase peptide amide synthesis. Fast couplings with high fidelity were achieved enabling the synthesis of selected conotoxins that previously demonstrated artificially ‘difficult sequences’ on commercially available p-MBHA resins.

    3. You have free access to this content
      Native chemical ligation of hydrophobic peptides in organic solvents (pages 558–562)

      Marc Dittmann, Jörg Sauermann, Ralf Seidel, Wolfgang Zimmermann and Martin Engelhard

      Version of Record online: 2 SEP 2010 | DOI: 10.1002/psc.1285

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      Native chemical ligations can be carried out efficiently and fast in organic solvents like dimethylformamide. These conditions are suitable for the synthesis of hydrophobic peptides and possibly membrane proteins.

  4. Rapid Communications

    1. Top of page
    2. Editorials
    3. Reviews
    4. Research Articles
    5. Rapid Communications
    6. Research Articles
    1. Phosphoramidate-peptide synthesis by solution- and solid-phase Staudinger-phosphite reactions (pages 563–567)

      Remigiusz A. Serwa, Jean-Marie Swiecicki, Denise Homann and Christian P. R. Hackenberger

      Version of Record online: 14 MAY 2010 | DOI: 10.1002/psc.1236

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      The chemoselective incorporation of phosphoramidate moieties into peptides by a Staudinger-phosphite reaction of azides can be performed in many solvents, including water. In this report, we present two strategies for an efficient synthesis of phosphoramidate-containing peptides, in which the Staudinger-phosphite reaction is performed either on the solid support or in solution with aryl azido-containing peptides. The corresponding Staudinger reactions proceed in high conversion rates and deliver phosphoramidate peptides, in which the modification site is located in the middle of the peptide sequence.

  5. Research Articles

    1. Top of page
    2. Editorials
    3. Reviews
    4. Research Articles
    5. Rapid Communications
    6. Research Articles
    1. Selective labelling of stromal cell-derived factor 1α with carboxyfluorescein to study receptor internalisation (pages 568–574)

      Kathrin Bellmann-Sickert, Lars Baumann and Annette G. Beck-Sickinger

      Version of Record online: 6 APR 2010 | DOI: 10.1002/psc.1228

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      Stromal cell-derived factor 1α was selectively modified with carboxyfluorescein by expressed protein ligation. Receptor activation, specific binding and internalisation are demonstrated.

    2. Protein trans-splicing on an M13 bacteriophage: towards directed evolution of a semisynthetic split intein by phage display (pages 575–581)

      Daniel Garbe, Ilka V. Thiel and Henning D. Mootz

      Version of Record online: 14 MAY 2010 | DOI: 10.1002/psc.1243

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      Protein trans-splicing has recently received increasing attention for the semisynthesis of proteins. We report that a semisynthetic protein can be generated on the surface of an M13 bacteriophage using an artificially split Ssp DnaB intein. This finding will provide the basis for improving split inteins as ligation tools by directed evolution and phage display.

    3. Protein immobilization on liposomes and lipid-coated nanoparticles by protein trans-splicing (pages 582–588)

      Nam Ky Chu, Diana Olschewski, Ralf Seidel, Konstanze F. Winklhofer, Jörg Tatzelt, Martin Engelhard and Christian F. W. Becker

      Version of Record online: 6 APR 2010 | DOI: 10.1002/psc.1227

      Thumbnail image of graphical abstract

      A synthetic double lipidated peptide linked to a C-terminal split intein domain serves as an efficient membrane anchor for selective immobilization of target proteins expressed in fusion with an N-terminal split intein domain on vesicles and lipid coated nanoparticles via protein trans-splicing.

    4. Azatryptophans as tools to study polarity requirements for folding of green fluorescent protein (pages 589–595)

      Michael Georg Hoesl, Maud Larregola, Haissi Cui and Nediljko Budisa

      Version of Record online: 13 JUL 2010 | DOI: 10.1002/psc.1263

      Thumbnail image of graphical abstract

      In vivo translation of non-canonical amino acids is closely connected to the folding of the related protein product. This is well documented with green fluorescent proteins by substitution of Trp residues with the isosteric and hydrophilic azatryptophan analogs. The results point to an intriguing correlation between the physicochemical nature of translated non-canonical amino acid and subsequent in vivo protein folding.

    5. Temperature-induced transition between polyproline I and II helices: quantitative fitting of hysteresis effects (pages 596–600)

      Michael Kuemin, Jürgen Engel and Helma Wennemers

      Version of Record online: 2 JUN 2010 | DOI: 10.1002/psc.1245

      Thumbnail image of graphical abstract

      A conformational transition from the PPI helix to the PPII helix takes place upon heating oligoprolines, and back to the PPII helix upon cooling. The transitional loop is characterized by a strong hysteresis which was fitted quantitatively by a newly developed kinetic formalism.

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