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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  • Charge neutralization in the active site of the catalytic trimer of aspartate transcarbamoylase promotes diverse structural changes

    Charge neutralization in the active site of the catalytic trimer of aspartate transcarbamoylase promotes diverse structural changes

    Feature-enhanced electron density map of the active-site region containing the R105A substitution with residue A105 omitted from the map calculation. The map, which is shown at a contour level of 1.0σ, shows density consistent with an alanine residue at position 105, which is shown in a thicker stick representation. The map was generated using PHENIX and the figure was rendered using PyMOL (https://www.pymol.org)

  • Homology modeling in a dynamical world

    Homology modeling in a dynamical world

    MSD distributions over all homologous protein pairs by bins of 10% sequence identity. Above and below the median (horizontal line inside each box) are the first and third quartiles, respectively. The notches display the median absolute deviation.

  • Cyclic oligomer design with de novo αβ-proteins

    Cyclic oligomer design with de novo αβ‐proteins

    Crystal structure of design C2_Fd_7A_8. (Left panel) (A) Computational design model (yellow) aligned with crystal structure (light blue) with aliphatic residues at interface from one monomer shown. The helix at the interface was designed to bend toward the interacting helix in design model and the bending is even more significant in crystal structure. (B) (C) (D) (E) Close-up view of L27, I23, L16, and L12 respectively. Due to the increase curvature, side chains are packed deeper into the interface core in crystal structure. (Right panel) Backbone superimposition of Fd_7A (pink), computational design model (yellow) and crystal structure (light blue) of C2_Fd_7A_8 chain A

  • Building collagen IV smart scaffolds on the outside of cells

    Building collagen IV smart scaffolds on the outside of cells

    Collagen IV functions as a smart scaffold. Binding motifs are embedded along the length of the triple helix for binding integrins, and various macromolecules. This protein complex influences cell adhesion, migration, development, tissue regeneration, wound healing, and plays a role in molecular sieving.

  • Amyloidogenesis of Tau protein

    Amyloidogenesis of Tau protein

    Amyloid fibrils of Tau visualized by TEM. Recombinant human Tau forms polymorphic fibrils in vitro. These assemblies may resemble amyloid fibrils found in tauopathies. (A) SFs formed by recombinant human full-length Tau (2N4R, 441 amino acids). (B) PHFs formed by the K18 peptide. The scale bar is 100 nm

  • Crowd sourcing difficult problems in protein science*

    Crowd sourcing difficult problems in protein science*

    Screenshot of Foldit during one of the learning tutorials. Foldit uses color cues and structural simplification to provide important information to players without overwhelming them. The tutorials provide text-box clues with information about the game in order to familiarize players with the mechanics. In Foldit, players are tasked with achieving the highest score, which corresponds to the most favorable three-dimensional conformation of a protein

  • Charge neutralization in the active site of the catalytic trimer of aspartate transcarbamoylase promotes diverse structural changes
  • Homology modeling in a dynamical world
  • Cyclic oligomer design with de novo αβ‐proteins
  • Building collagen IV smart scaffolds on the outside of cells
  • Amyloidogenesis of Tau protein
  • Crowd sourcing difficult problems in protein science*

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Author Suzanne Scarlata on her recently published Protein Science paper entitled "Regulation of the Activity of the Promoter of RNA-induced Silencing, C3PO." 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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