Protein Science

Cover image for Vol. 26 Issue 3

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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  • Novel product specificity toward erlose and panose exhibited by multisite engineered mutants of amylosucrase

    Novel product specificity toward erlose and panose exhibited by multisite engineered mutants of amylosucrase

    Molecular docking of erlose in wild-type NpAS and its mutants 47A10, 37G4, and 39A8. Mutated positions are shown and coloured depending on the loop they belong to. Loops 3, 4, 5, and 7 are colored in magenta, blue, yellow and green, respectively. Labelled in white are highlighted commonly mutated positions and in black are shown mutated positions that are specific to the mutants. Catalytic residues are shown in ball and stick.

  • Exploring the potential of boronic acids as inhibitors of OXA-24/40 β-lactamase

    Exploring the potential of boronic acids as inhibitors of OXA‐24/40 β‐lactamase

    Superposition of BA4 and BA16. Edge-to-face trimer aromatic interactions between the benzoxaborole BA4, Tyr112, and Trp115 are indicated with purple dashed lines between the centroid atom positions of the aryl rings.

  • The membrane localization domains of two distinct bacterial toxins form a 4-helix-bundle in solution

    The membrane localization domains of two distinct bacterial toxins form a 4‐helix‐bundle in solution

    Alignment of top 20 solution structures of MLDPMT and MLDRRSP. Three-dimensional superposition of the top 20 structures of MLDPMT (A) and MLDRRSP (B), as determined using solution state NMR. The backbone RMSD of the helix residues of MLDPMT is 0.99 Å and of MLDRRSP is 0.96 Å.

  • Formation and carbon monoxide-dependent dissociation of Allochromatium vinosum cytochrome c′ oligomers using domain-swapped dimers

    Formation and carbon monoxide‐dependent dissociation of Allochromatium vinosum cytochrome c′ oligomers using domain‐swapped dimers

    Superimposed figure of the active site structures of the AVCP native dimer (PDB code: 1BBH) and tetramer (PDB code: 5GYR). The monomer and domain-swapped dimer subunits of the tetramer are depicted in green and red/blue, respectively. The red and blue regions in the domain-swapped dimer correspond to different protomers. The native dimer is depicted in orange. The hemes and the side chain atoms of Tyr16, heme-binding Cys121 and Cys124, and heme iron-coordinating His125 are shown as stick models. The sulfur atoms of the side chains of Cys121 and Cys124 are depicted in yellow, the nitrogen atoms of the side chain of His125 are depicted in blue, and the oxygen atom of the side chain of Tyr16 is depicted in red.

  • A cell is more than the sum of its (dilute) parts: A brief history of quinary structure

    A cell is more than the sum of its (dilute) parts: A brief history of quinary structure

    Five levels of protein structure by Chris A. Pielak. The tertiary and quanternary structures are based the B1 domain of protein G (PDB entries 1GB1 and 2RMM).

  • On the appearance of carboxylates in electrostatic potential maps

    On the appearance of carboxylates in electrostatic potential maps

    Simulated ESP maps for Asp side chain in protonated state (A), deprotonated-delocalized state (B), and deprotonated-non-delocalized state at 2.0 Å (top) and 3.0 Å resolution (bottom), contoured at +5.0σ (cyan), +10.0σ (gold), and/or +15.0σ (blue).

  • Novel product specificity toward erlose and panose exhibited by multisite engineered mutants of amylosucrase
  • Exploring the potential of boronic acids as inhibitors of OXA‐24/40 β‐lactamase
  • The membrane localization domains of two distinct bacterial toxins form a 4‐helix‐bundle in solution
  • Formation and carbon monoxide‐dependent dissociation of Allochromatium vinosum cytochrome c′ oligomers using domain‐swapped dimers
  • A cell is more than the sum of its (dilute) parts: A brief history of quinary structure
  • On the appearance of carboxylates in electrostatic potential maps

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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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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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