Protein Science

Cover image for Vol. 26 Issue 4

Edited By: Brian W. Matthews

Impact Factor: 3.039

ISI Journal Citation Reports © Ranking: 2015: 118/289 (Biochemistry & Molecular Biology)

Online ISSN: 1469-896X

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  • Epitope mapping of Borrelia burgdorferi OspC protein in homodimeric fold

    Epitope mapping of Borrelia burgdorferi OspC protein in homodimeric fold

    Determined localization of epitopes mapped into the OspC dimer structure (pdb entry 1ggq).

  • Molecular mechanisms underlying deoxy-ADP.Pi activation of pre-powerstroke myosin

    Molecular mechanisms underlying deoxy‐ADP.Pi activation of pre‐powerstroke myosin

    Loss of O2' disrupts contacts in the nucleotide binding pocket. Representative figures showing the conformation of the nucleotide binding pocket at both 0 and 50 ns from ADP.Pi and dADP.Pi simulations. The isolated sphere represents the magnesium ion. Phe129 is highlighted in magenta, and the primary contacts it makes are shown with a dotted black line in the 50 ns figures.

  • Structural and functional insights into thermally stable cytochrome c′ from a thermophile

    Structural and functional insights into thermally stable cytochrome c′ from a thermophile

    A. Overall dimeric structure of PHCP. The main chain and heme are presented as ribbon and stick models, respectively. The single subunits are colored red and orange. The N- and C- termini as well as helical regions in each subunit are indicated. B. A channel to the sixth coordinate position of the heme for the ligand-binding ability in PHCP. A single subunit of PHCP is shown with a red surface. The heme is shown as a stick model.

  • High resolution crystal structures of human kynurenine aminotransferase-I bound to PLP cofactor, and in complex with aminooxyacetate

    High resolution crystal structures of human kynurenine aminotransferase‐I bound to PLP cofactor, and in complex with aminooxyacetate

    View of the active site and interaction of the AOAA with hKAT-1 superimposed on the native structure. Carbon atoms are colored according to their structural origins: on the PLP colored mauve, native structure blue and AOAA inhibited structure green. Figure was created with PyMOL.

  • Modulating the wnt signaling pathway with small molecules

    Modulating the wnt signaling pathway with small molecules

    2-D structures of GSK-3β inhibitors, which result in activation of the Wnt pathway.

  • SSB and the RecG DNA helicase: an intimate association to rescue a stalled replication fork

    SSB and the RecG DNA helicase: an intimate association to rescue a stalled replication fork

    Organization of the SSB protein. (A) Schematic of SSB divided into the core and tail regions by proteolytic cleavage. The conservation scores for each region were calculated from alignments using Praline. The pI of each region is shown in red and was calculated using the ProtParam tool of Expasy. The pI of the intact protein is 5.44. (B) The SSB tetramer is intimately associated with ssDNA. The image was generated using PDB file 1EYG. The DNA is colored green and the tetramer, shown as a ribbon, is colored purple. (C) The linker domain of SSB can adopt different conformations. The image was generated using PDB file 1QVC. Each subunit is presented in a different color with C-termini labelled in red.

  • Epitope mapping of Borrelia burgdorferi OspC protein in homodimeric fold
  • Molecular mechanisms underlying deoxy‐ADP.Pi activation of pre‐powerstroke myosin
  • Structural and functional insights into thermally stable cytochrome c′ from a thermophile
  • High resolution crystal structures of human kynurenine aminotransferase‐I bound to PLP cofactor, and in complex with aminooxyacetate
  • Modulating the wnt signaling pathway with small molecules
  • SSB and the RecG DNA helicase: an intimate association to rescue a stalled replication fork

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Author Shigeki Arai on his recently published Protein Science paper entitled " An insight into the thermodynamic characteristics of human thrombopoietin complexation with TN1 antibody." Read the paper here

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Protein Science Awards

2017 Best Paper Award

2017 Best Paper Award Winners
We are pleased to announce the winners of the 2017 Protein Science Best Paper Award:

Charlotte Miton
Postdoctoral Research Fellow
Michael Smith Laboratories at University of British Columbia

How mutational epistasis impairs predictability in protein evolution and design
Charlotte M. Miton and Nobuhiko Tokuriki
Protein Sci. 25:1260-1272, 2016.

Zach Schaefer
Graduate Student
Department of Biochemistry and Molecular Biology at University of Chicago

A polar ring endows improved specificity to an antibody fragment
Zachary P. Schaefer, Lucas J. Bailey and Anthony A. Kossiakoff
Protein Sci. 25:1290-1298, 2016.

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2017 Young Investigator Award Winner

The Protein Science Young Investigator Award recognizes a scientist generally within the first 8 years of an independent career who has made an important contribution to the study of proteins. The 2017 winner is Dr. David Pagliarini (University of Wisconsin, Madison).

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More information on our awards can be found here.

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