Protein Science

Cover image for Vol. 26 Issue 12

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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  • The unique N-terminal zinc finger of synaptotagmin-like protein 4 reveals FYVE structure

    The unique N‐terminal zinc finger of synaptotagmin‐like protein 4 reveals FYVE structure

    Structural comparisons with the Slp4N peptide. Ribbon diagrams of (A) the lowest energy structure of the Slp4N peptide, showing the heavy atoms of the side chains of the hydrophobic core residues and eight zinc ligating-residues; (B) the RING structure of EL5; and (C) the FYVE structure of Vps27p. Zinc atoms, β strands, and α-helices are shown in magenta, blue, and red, respectively. (D) Structural alignments of the Slp4N peptide, the RING structure of EL5, and the FYVE structure of Vps27p with secondary structure elements, where the stars represent the highly conserved residues provided by GREMLIN. Zinc ligands are shown in red.

  • Protein–protein interactions leave evolutionary footprints: High molecular coevolution at the core of interfaces

    Protein–protein interactions leave evolutionary footprints: High molecular coevolution at the core of interfaces

    Score distribution of the Interface Core residues. Conservation (Cons) and cMI scores were normalized to fall in the range [0–1]. The plot shows the score distribution of Interface Core residues in the dataset (32,934 residues). We considered 0.5 as the threshold between high and low scores (black lines). The majority of points (67.48% residues) shows low scores (cMI <0.5 and Cons < 0.5). Only 3.09% of the residues have high cMI and Conservation scores.

  • Crystal structure of the Legionella pneumophila Lpg2936 in complex with the cofactor S-adenosyl-L-methionine reveals novel insights into the mechanism of RsmE family methyltransferases

    Crystal structure of the Legionella pneumophila Lpg2936 in complex with the cofactor S‐adenosyl‐L‐methionine reveals novel insights into the mechanism of RsmE family methyltransferases

    Cartoon representation of the monomeric Lpg2936. The N-terminal and C-terminal domains are indicated as NTD and CTD and colored in lightblue and blue, respectively. N and C-terminal residues of the chain as well as the secondary structure elements are indicated. The bound AdoMet molecule is represented as sticks. Two orientations are shown rotated by 90°.

  • How does the exosite of rhomboid protease affect substrate processing and inhibition?

    How does the exosite of rhomboid protease affect substrate processing and inhibition?

    Two projections on the overlapping of P6 – P5' residues of 11-pep (red) and 33-pep (yellow) substrates. Superposition on S201 and H254 backbone atoms of GlpG in the pre-catalytic non-covalent complex.

  • The bulky and the sweet: How neutralizing antibodies and glycan receptors compete for virus binding

    The bulky and the sweet: How neutralizing antibodies and glycan receptors compete for virus binding

    Schematic representation of the competition between antibodies and glycan receptors for virus binding. Exemplified is a virus with trimeric spike proteins shown in gray and an antibody with heavy and light chain in dark and light purple, respectively. Cell-surface carbohydrates (built with web-based glycan modeler tools of: Woods Group [2005–2017] GLYCAM Web. Complex Carbohydrate Research Center, University of Georgia, Athens, GA. [http://glycam.org]) are shown in a schematic representation and are roughly scaled to the size of the viral spikes and antibody.

  • From chaperonins to Rubisco assembly and metabolic repair

    From chaperonins to Rubisco assembly and metabolic repair

    The process of photosynthesis converts sunlight into chemical energy, splits water to liberate O2, and fixes CO2 into sugar. The light reactions provide energy and reducing agents (ATP and NADPH), which are used in the light-independent Calvin-Benson-Bassham (CBB) cycle. The enzyme Rubisco catalyzes the key step of fixation of atmospheric CO2 by mediating the carboxylation of the 5-carbon sugar substrate ribulose-1,5-bisphosphate (RuBP)

  • The unique N‐terminal zinc finger of synaptotagmin‐like protein 4 reveals FYVE structure
  • Protein–protein interactions leave evolutionary footprints: High molecular coevolution at the core of interfaces
  • Crystal structure of the Legionella pneumophila Lpg2936 in complex with the cofactor S‐adenosyl‐L‐methionine reveals novel insights into the mechanism of RsmE family methyltransferases
  • How does the exosite of rhomboid protease affect substrate processing and inhibition?
  • The bulky and the sweet: How neutralizing antibodies and glycan receptors compete for virus binding
  • From chaperonins to Rubisco assembly and metabolic repair

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Authors Melanie Dietrich, Christina Harprecht and Thilo Stehle on their recently published Protein Science paper entitled "The bulky and the sweet: How neutralizing antibodies and glycan receptors compete for virus binding." Read the paper here

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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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