Protein Science

Cover image for Vol. 26 Issue 6

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 and biochemical characterization of the nucleoside hydrolase from C. elegans reveals the role of two active site cysteine residues in catalysis

    Structural and biochemical characterization of the nucleoside hydrolase from C. elegans reveals the role of two active site cysteine residues in catalysis

    Active site arrangement of CeNH. (A) Close up view of the CeNH active site showing the bound Tris molecule and Ca2+ ion. The residues and the Tris molecule are shown in stick representation with differently colored carbon atoms. The Ca2+ ion is shown as a red sphere. A Ca2+-interacting water molecule, corresponding to the nucleophile and three Tris interacting water molecules are shown as cyan spheres. Residues interacting with the Tris molecules are shown as sticks and the hydrogen bonds as dotted lines. Residues interacting with the Ca2+ ion are not shown. (B) Electrostatic potential surface around the active site cavity of CeNH. The bound Tris molecule is shown in sticks representation. The position of the two active site regions, “loop1” and “loop2” is indicated.

  • Crystal structure of human proteasome assembly chaperone PAC4 involved in proteasome formation

    Crystal structure of human proteasome assembly chaperone PAC4 involved in proteasome formation

    Surface potential representation of (A) human and (B) yeast proteasomal α4 and α5 subunits and the assembly chaperones PAC4/Pba4. The surface models of human (5LE5) and yeast (1RYP) proteasomal α4/α5 complexes (left) and PAC4 orthologs (right) are colored according to the electrostatic surface potential (blue, positive; red, negative). The human α4/α5–PAC4 and yeast α4/α5–Pba4 are shown in an open-book representation.

  • Characterization of structural and immunological properties of a fusion protein between flagellin from Salmonella and lumazine synthase from Brucella

    Characterization of structural and immunological properties of a fusion protein between flagellin from Salmonella and lumazine synthase from Brucella

    Three-dimensional structure of the decameric BLS (PDB code: 1T13), the flagellin 131 (PDB code: 3A5X), and a model of BLS-FliC131 chimera. The structures are represented as surface and for BLS and flagellin also as cartoon. The expected MW values are indicated.

  • Structural and dynamic characterization of a freestanding acyl carrier protein involved in the biosynthesis of cyclic lipopeptide antibiotics

    Structural and dynamic characterization of a freestanding acyl carrier protein involved in the biosynthesis of cyclic lipopeptide antibiotics

    Differences of the protection factors between apo- and holo-LipD obtained from the H/D exchange are plotted on the apo-LipD structure. Residues with red color had a slower H/D exchange rate in holo-LipD.

  • Monobodies and other synthetic binding proteins for expanding protein science

    Monobodies and other synthetic binding proteins for expanding protein science

    Examples of Monobodies and Adnectins binding to a functional site within the target protein. The target proteins are shown in gray with the epitope in orange. Natural ligands are in red, and Monobodies and Adnectins in blue. The identities of the target molecules and PDB entry codes are indicated. For the Fluc channel structure, the natural ligand, F– ion, is not shown because of its small size.

  • Breaking up and making up: The secret life of the vacuolar H+-ATPase

    Breaking up and making up: The secret life of the vacuolar H+‐ATPase

    Interactions at the V1–Vo interface. (A) The affinities of the individual interactions have been measured using isothermal titration calorimetry of recombinant yeast V-ATPase subunits. (B) Spring-loading of EG3. It has been suggested that the tension in EG3 would prevent re-forming of the EG2–aNT(distal)–Cfoot ternary interface after one of these interactions is broken to initiate disassembly.

  • Structural and biochemical characterization of the nucleoside hydrolase from C. elegans reveals the role of two active site cysteine residues in catalysis
  • Crystal structure of human proteasome assembly chaperone PAC4 involved in proteasome formation
  • Characterization of structural and immunological properties of a fusion protein between flagellin from Salmonella and lumazine synthase from Brucella
  • Structural and dynamic characterization of a freestanding acyl carrier protein involved in the biosynthesis of cyclic lipopeptide antibiotics
  • Monobodies and other synthetic binding proteins for expanding protein science
  • Breaking up and making up: The secret life of the vacuolar H+‐ATPase

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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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