Protein Science

Cover image for Vol. 27 Issue 3

Edited By: Brian W. Matthews

Impact Factor: 2.523

ISI Journal Citation Reports © Ranking: 2016: 160/290 (Biochemistry & Molecular Biology)

Online ISSN: 1469-896X

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  • Concerted millisecond timescale dynamics in the intrinsically disordered carboxyl terminus of γ-tubulin induced by mutation of a conserved tyrosine residue

    Concerted millisecond timescale dynamics in the intrinsically disordered carboxyl terminus of γ‐tubulin induced by mutation of a conserved tyrosine residue

    Visualization of the full γ-TURC with the compact (A) and extended (B) conformation of the γ-CT sampled during the MC simulations. Structure of the γ-TURC is taken from pdb 5FLZ. The compact and extended conformations of the γ-CT correspond to radii of gyration of 11.9 and 23.5 Å, respectively. Protein structures are shown as spheres. The γ-Tu, γ-CT, SPC97, SPC98, and SPC110 and are colored in gold, pink, cyan, blue, and light green, respectively.

  • Evidence for multiple modes of neutrophil serine protease recognition by the EAP family of Staphylococcal innate immune evasion proteins

    Evidence for multiple modes of neutrophil serine protease recognition by the EAP family of Staphylococcal innate immune evasion proteins

    Sequence differences explain the failure of EapH1 and EapH2 to bind the NSP homolog, azurocidin. (A) Representation of the EapH1/NE complex where EapH1 is drawn as a teal ribbon and NE is shown as a grey molecular surface. Residues of the NE catalytic triad are colored magenta for the purposes of orientation. (B) Structural superposition of NE and AZU, where NE is drawn a grey wire and AZU as a purple wire. Note the extensive structural homology shared by the chymotrypsin fold. (C) NE shown as a molecular surface, where the EapH1 interfacing residues are colored in orange. (D) NE shown as a molecular surface, where the residues that differ between NE and AZU are colored in purple. (E) NE shown as a molecular surface where the residues that differ between NE and AZU are colored purple, while those residues that are the same and are found at the EapH1 interface are colored orange. (F) An identical representation to panel E, except that EapH1 is shown in cyan as it lies in the EapH1/NE complex.

  • The structure of glucose-1-phosphate thymidylyltransferase from Mycobacterium tuberculosis reveals the location of an essential magnesium ion in the RmlA-type enzymes

    The structure of glucose‐1‐phosphate thymidylyltransferase from Mycobacterium tuberculosis reveals the location of an essential magnesium ion in the RmlA‐type enzymes

    Superposition of the ligands in the RmlA/dTTP and the RmlA/dTDP-glucose complexes. The dTDP-glucose is highlighted in violet bonds whereas the dTTP is colored in cyan.

  • Folding nucleus structure persists in thermally-aggregated FGF-1

    Folding nucleus structure persists in thermally‐aggregated FGF‐1

    2D-fpRFDR spectra of aggregated FGF-1. The 2D-fpRFDR spectrum of C, N uniformly labeled aggregated FGF-1. The off-diagonal cross-peaks correspond to correlations between covalently bonded C atoms. Colored horizontal and vertical lines indicate assignment of cross-peaks based on amino acid type, indicated by single-letter abbreviations.

  • Characterization of and lipopolysaccharide binding to the E. coliLptC protein dimer

    Characterization of and lipopolysaccharide binding to the E. coliLptC protein dimer

    LptC N-terminal dimer supported by the DEER data (pdb: 4B54). (A) Sites spin labeled for DEER spectroscopy studies on the LptC dimer orientation viewed straight down onto the dimer interface. The unresolved N- and C-terminal residues of the crystal structure are represented by dotted lines. N indicates the N-terminus and C denotes the location of the C-terminus. (B) The LptC dimer structure from A rotated to view the side of the dimer interface. Distances experimentally derived from the DEER data presented in Figure are indicated for each site.

  • A structural overview of mycobacterial adhesins: Key biomarkers for diagnostics and therapeutics

    A structural overview of mycobacterial adhesins: Key biomarkers for diagnostics and therapeutics

    Structures of Fibronectin-binding adhesins. Cartoon representations of the structures of (A) Ag85A, belonging to the antigen 85 complex. The protein surface is also drawn to evidence fibronectin binding region (1–30, 39–66, and 98–111, orange); (B) malate synthase GlcB. The C-terminal domain involved in fibronectin binding is drawn in red; (C) Gln synthase dodecamer.

  • Concerted millisecond timescale dynamics in the intrinsically disordered carboxyl terminus of γ‐tubulin induced by mutation of a conserved tyrosine residue
  • Evidence for multiple modes of neutrophil serine protease recognition by the EAP family of Staphylococcal innate immune evasion proteins
  • The structure of glucose‐1‐phosphate thymidylyltransferase from Mycobacterium tuberculosis reveals the location of an essential magnesium ion in the RmlA‐type enzymes
  • Folding nucleus structure persists in thermally‐aggregated FGF‐1
  • Characterization of and lipopolysaccharide binding to the E. coliLptC protein dimer
  • A structural overview of mycobacterial adhesins: Key biomarkers for diagnostics and therapeutics

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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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