S
S.J. Remington
Researcher at University of Oregon
Publications - 46
Citations - 6044
S.J. Remington is an academic researcher from University of Oregon. The author has contributed to research in topics: Citrate synthase & Protein structure. The author has an hindex of 32, co-authored 46 publications receiving 5832 citations. Previous affiliations of S.J. Remington include Max Planck Society.
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Journal ArticleDOI
Crystallographic and energetic analysis of binding of selected anions to the yellow variants of green fluorescent protein.
TL;DR: In this paper, the authors solved apo and I(-)-bound crystal structures of YFP-H148Q to 2.1 A resolution, showing that the halide-binding site is found near van der Waals contact with the chromophore imidazolinone oxygen atom, in a small buried cavity adjacent to Arg96, which provides electrostatic stabilization.
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Kindling fluorescent protein from Anemonia sulcata: dark-state structure at 1.38 A resolution.
M.L. Quillin,David M. Anstrom,Xiaokun Shu,Shannon O'Leary,K. Kallio,D.M. Chudakov,S.J. Remington +6 more
TL;DR: The crystal structure of the "kindling fluorescent protein" asFP595-A143G (KFP) in the dark-adapted state at 1.38 A resolution and 100 K is determined and the energy barrier for thermal relaxation was found to be somewhat higher than the value of approximately 55 kJ/mol observed for cis-trans isomerization of a model chromophore in solution.
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Structure of the lysozyme from bacteriophage T4: An electron density map at 2.4 Å resolution
S.J. Remington,Wayne F. Anderson,Joyce Emrich Owen,L. F. Ten Eyck,C T Grainger,Brian W. Matthews +5 more
TL;DR: The three-dimensional structure of the lysozyme from bacteriophage T4 has been determined from a 2.4 A resolution electron density map and the approximate conformation of the molecule unambiguously is revealed.
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Refined atomic model of wheat serine carboxypeptidase II at 2.2-A resolution.
TL;DR: A comparison of the active site features of the three families of serine proteinases suggests that the "catalytic triad" should actually be regarded as two diads, a His-Asp diad and a his-Ser diad, and that the relative orientation of one diad with respect to the other is not particularly important.
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Comparison of goose-type, chicken-type, and phage-type lysozymes illustrates the changes that occur in both amino acid sequence and three-dimensional structure during evolution.
TL;DR: Comparisons of goose-type, chicken- type, and phage-type lysozymes are made to suggest that all three classes of lysozyme diverged from a common evolutionary precursor, even though their amino acid sequences appear to be unrelated.