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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  • Recognition of corn defense chitinases by fungal polyglycine hydrolases

    Recognition of corn defense chitinases by fungal polyglycine hydrolases

    Structure of the Es-cmp binding site. The four amino acids, identified as important for protease recognition in this study, were modeled onto the truncated ChitA structure (red cartoon) as blue sticks.

  • Structure of 6-diazo-5-oxo-norleucine-bound human gamma-glutamyl transpeptidase 1, a novel mechanism of inactivation

    Structure of 6‐diazo‐5‐oxo‐norleucine‐bound human gamma‐glutamyl transpeptidase 1, a novel mechanism of inactivation

    Crystal structure of DON-bound hGGT1. A stereo ribbon presentation of the hGGT1 heterodimer with DON bound in the active site (5V4Q). The large subunit (chain A) is colored blue, and the small subunit (chain B) is colored green. Thr381, the N-terminus of the small subunit, is shown as a green stick figure. The DON atoms are colored red (the diazo group of DON is released when DON binds to the enzyme and is not present in the final structure).

  • Activation mechanisms of the first sphingosine-1-phosphate receptor

    Activation mechanisms of the first sphingosine‐1‐phosphate receptor

    Cross Correlation of the Active Trajectories. The top triangle is the difference of correlation between the active trajectories compared to the cMD antagonist-bound control. The lower triangle is the cross correlation values of the active trajectories.

  • Activation mechanisms of αVβ3 integrin by binding to fibronectin: A computational study

    Activation mechanisms of αVβ3 integrin by binding to fibronectin: A computational study

    Dynamical cross-correlation maps to compare the degree of correlated motion of the residues in αV and β3 subunit of integrin αVβ3 bound with fibronectin (bottom-right) and without bound to fibronectin (top-left).

  • Intrinsically disordered inhibitor of glutamine synthetase is a functional protein with random-coil-like pKa values

    Intrinsically disordered inhibitor of glutamine synthetase is a functional protein with random‐coil‐like pKa values

    Simulated protein conformations. (A) Ensemble of structures sampled at 1 ns in the time interval 30-40 ns (color scale is from blue to red); MultiProt was used for molecule superposition. (B) Protein snapshot representing the average conformation, with helical structure and acidic residues explicitly shown; the N-terminus is on the upper left and the C-terminus on the right.

  • On contribution of known atomic partial charges of protein backbone in electrostatic potential density maps

    On contribution of known atomic partial charges of protein backbone in electrostatic potential density maps

    Averaged experimental ESP density maps. A: Using four non-H atoms of 20 four-atom peptide units in averaging, contoured at +10σ (cyan), +15σ (salmon), +20σ (blue), and +25σ (green). B: Using 20 five-atom peptide units in averaging. C: Averaged experimental ESP map for 20 five-atom chiral Cα centers in four different views contoured at +15σ (salmon), +19σ (blue), and +23σ (cyan).

  • Recognition of corn defense chitinases by fungal polyglycine hydrolases
  • Structure of 6‐diazo‐5‐oxo‐norleucine‐bound human gamma‐glutamyl transpeptidase 1, a novel mechanism of inactivation
  • Activation mechanisms of the first sphingosine‐1‐phosphate receptor
  • Activation mechanisms of αVβ3 integrin by binding to fibronectin: A computational study
  • Intrinsically disordered inhibitor of glutamine synthetase is a functional protein with random‐coil‐like pKa values
  • On contribution of known atomic partial charges of protein backbone in electrostatic potential density 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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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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