J
Joel Berendzen
Researcher at Los Alamos National Laboratory
Publications - 45
Citations - 10315
Joel Berendzen is an academic researcher from Los Alamos National Laboratory. The author has contributed to research in topics: Myoglobin & Structural genomics. The author has an hindex of 29, co-authored 44 publications receiving 10014 citations. Previous affiliations of Joel Berendzen include University of Vermont & University of Illinois at Urbana–Champaign.
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Journal ArticleDOI
Automated MAD and MIR structure solution
TL;DR: A fully automated procedure for solving MIR and MAD structures has been developed using a scoring scheme to convert the structure-solution process into an optimization problem.
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The Catalytic Pathway of Cytochrome P450Cam at Atomic Resolution
Ilme Schlichting,Joel Berendzen,Kelvin Chu,Kelvin Chu,Ann M. Stock,Shelley A. Maves,David E. Benson,Robert M. Sweet,Dagmar Ringe,Gregory A. Petsko,Stephen G. Sligar,Stephen G. Sligar +11 more
TL;DR: Structures were obtained for three intermediates in the hydroxylation reaction of camphor by P450cam with trapping techniques and cryocrystallography and reveal a network of bound water molecules that may provide the protons needed for the reaction.
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Rapid protein-folding assay using green fluorescent protein.
TL;DR: This work demonstrated that the fluorescence of Escherichia coli cells expressing GFP fusions is related to the productive folding of the upstream protein domains expressed alone, providing a simple route to improving protein folding and expression by directed evolution.
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Protein states and proteinquakes
Anjum Ansari,Joel Berendzen,S F Bowne,Hans Frauenfelder,Icko Iben,Todd B. Sauke,E. Shyamsunder,Robert D. Young +7 more
TL;DR: Investigation of the proteinquake and of related intramolecular equilibrium motions shows that states and motions have a hierarchical glass-like structure.
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A unified model of protein dynamics.
Hans Frauenfelder,Guo Chen,Joel Berendzen,Paul W. Fenimore,Helén Jansson,Benjamin H. McMahon,Izabela Stroe,Jan Swenson,Robert D. Young +8 more
TL;DR: It is shown here that the dominant conformational motions are slaved by the hydration shell and the bulk solvent, and the model quantitatively predicts the rapid increase of the mean-square displacement above ≈200 K and explains the nonexponential time dependence of the protein relaxation after photodissociation.