Protein Science

Cover image for Vol. 25 Issue 12

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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  • Structural features of Cas2 from Thermococcus onnurineus in CRISPR-cas system type IV

    Structural features of Cas2 from Thermococcus onnurineus in CRISPR‐cas system type IV

    Overall structure properties of Ton_Cas2. A: Each protomer is represented by light magenta and white cartoons. Hydrophobic interactions and charge interactions are enlarged in the black dotted boxes, and interaction residues are indicated by sticks. B: Wide and open conformation of Ton_Cas2. The distance between the two Asp8 residues in dimer are enlarged in the black dotted box in superposed structures of promotor A with Sso_Cas2 (white) and Bha_Cas2 (wheat).

  • Crystal structure of zebrafish complement 1qA globular domain

    Crystal structure of zebrafish complement 1qA globular domain

    Overall structure of Dare-C1qAgD and its superposition with hC1qAgD. A: Dare-C1qAgD is a homotrimer composed of three molecules and numbered as A (yellow), B (magenta) and C (purple). Each monomer is composed of ten beta strands labeled A, A′, B′, B, and C–H. B: Superposition of three Dare-C1qAgD molecules showed the r.m.s.d. values of 0.132–0.152 Å based on their overall structures. C: Superposition of Dare-C1qAgD (yellow) and hC1qAgD (cyan) from the side view. The r.m.s.d. value between the two protein backbones is 0.561Å. Discrepant loops are indicated, including A-A′ loop (Dare-C1qAgD: residues 11-24) and D-E loop (Dare-C1qAgD: residues 69-73). A-A′ loop shows a 12.5Å shift and D-E loop shows a 14.3Å shift. D: Superposition of Dare-C1qAgD (yellow) and hC1qAgD (cyan) from the top view. Discrepant G-H loop (Dare-C1qAgD: residues 109-122) is indicated and shows a 33.9 Å shift.

  • Characterization of low affinity Fcγ receptor biotinylation under controlled reaction conditions by mass spectrometry and ligand binding analysis

    Characterization of low affinity Fcγ receptor biotinylation under controlled reaction conditions by mass spectrometry and ligand binding analysis

    Three-dimensional protein model of FcγRIIb with lysine residues indicated as colored amino acids. Below is the amino acid sequence of FcγRIIb with the IgG binding site from Hulett et al. in red and underlined and the lysine residues in blue.

  • Oxygen additions in serial femtosecond crystallographic protein structures

    Oxygen additions in serial femtosecond crystallographic protein structures

    Conventional σA-weighted F-map (contoured at +0.8σ, green) and ΔF-map (at +3.0σ, blue) for inserted O atoms.

  • An insight into the thermodynamic characteristics of human thrombopoietin complexation with TN1 antibody

    An insight into the thermodynamic characteristics of human thrombopoietin complexation with TN1 antibody

    The overall structure of TN1-Fab. (A) and (B) show the free TN1-Fab (PDB ID: 2ZKH, this work) and TN1-Fab–hTPO163 complex (PDB ID: 1V7M), respectively. For free TN1-Fab, the heavy and light chains are represented by red and yellow, respectively. For the TN1-Fab–hTPO163 complex, the heavy and light chains of TN1-Fab are represented by blue and green, respectively, and hTPO163 is depicted in gray. The dotted lines show the two pseudo-dyad axes generated by the superposition of CL on to CH1, and of VL on to VH.

  • Conformational flexibility of BECN1: Essential to its key role in autophagy and beyond

    Conformational flexibility of BECN1: Essential to its key role in autophagy and beyond

    Sequence alignment of BECN1 orthologs from diverse organisms. Increasing background color intensity corresponds to increasing residue conservation with red corresponding to invariant residues. Experimentally determined secondary structure is displayed above the alignment, with cylinders representing helices, arrows representing strands and lines representing coil, color-coded by domains as follows: IDR (black), BH3D (cyan), FHD (orange), CCD (magenta), and BARAD (green). Solid colors indicate natively folded stable structural elements, horizontal stripes indicate elements that may fold as part of two domains and diagonal stripes indicate binding-induced secondary structure. Anchor regions are boxed in black. Red triangles indicate the human NES.

  • Structural features of Cas2 from Thermococcus onnurineus in CRISPR‐cas system type IV
  • Crystal structure of zebrafish complement 1qA globular domain
  • Characterization of low affinity Fcγ receptor biotinylation under controlled reaction conditions by mass spectrometry and ligand binding analysis
  • Oxygen additions in serial femtosecond crystallographic protein structures
  • An insight into the thermodynamic characteristics of human thrombopoietin complexation with TN1 antibody
  • Conformational flexibility of BECN1: Essential to its key role in autophagy and beyond

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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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Special Issue in Honor of Ron Levy

Protein Science Awards

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2016 Best Paper Award Winners
We are pleased to announce the winners of the 2016 Protein Science Best Paper Award:

Tracy Clinton
Air Force Biochemist

Design and characterization of ebolavirus GP prehairpin intermediate mimics as drug targets
Tracy R. Clinton, Matthew T. Weinstock, Michael T. Jacobsen, Nicolas Szabo-Fresnais, Maya J. Pandya, Frank G. Whitby, Andrew S. Herbert, Laura I. Prugar, Rena McKinnon, Christopher P. Hill, Brett D. Welch, John M. Dye, Debra M. Eckert and Michael S. Kay
Protein Sci. 24:446-463, 2015.

Michael Thompson
Postdoctoral Fellow
Department of Bioengineering and Therapeutic Sciences at University of California, San Francisco

An allosteric model for control of pore opening by substrate binding in the EutL microcompartment shell protein
Michael C. Thompson, Duilio Cascio, David J. Leibly and Todd O. Yeates
Protein Sci. 24:956-975, 2015.

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2016 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 2016 winner is Dr. Benjamin Garcia (University of Pennsylvania Perelman School of Medicine).

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More information on our awards can be found here.

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