D
Dalibor Milić
Researcher at Paul Scherrer Institute
Publications - 40
Citations - 646
Dalibor Milić is an academic researcher from Paul Scherrer Institute. The author has contributed to research in topics: Crystal structure & Ligand. The author has an hindex of 15, co-authored 39 publications receiving 553 citations. Previous affiliations of Dalibor Milić include Max F. Perutz Laboratories & University of Düsseldorf.
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Journal ArticleDOI
Large-scale production and protein engineering of G protein-coupled receptors for structural studies.
TL;DR: Methods used for expression and purification of GPCRs for crystallographic and NMR studies are discussed and protein engineering methods that played a crucial role in obtaining GPCR crystal structures are summarized.
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Synthesis of five new molybdenum(VI) thiosemicarbazonato complexes. Crystal structures of salicylaldehyde and 3-methoxy-salicylaldehyde 4-methylthiosemicarbazones and their molybdenum(VI) complexes
Višnja Vrdoljak,Marina Cindrić,Dalibor Milić,Dubravka Matković-Čalogović,Predrag Novak,Boris Kamenar +5 more
TL;DR: In this paper, the results of the reaction of the [MoO2(acac)2] (acetylacetonate ligand, acac−, C5H7O2−) with 1 (salicylaldehyde 4-methylthiosemicarbazone ligand).
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Crystallographic Snapshots of Tyrosine Phenol-lyase Show That Substrate Strain Plays a Role in C–C Bond Cleavage
Dalibor Milić,Tatyana V. Demidkina,Nicolai G. Faleev,Robert S. Phillips,Dubravka Matković-Čalogović,Alfred A. Antson +5 more
TL;DR: X-ray structures for two enzymatic states that form just before and after the cleavage of the carbon–carbon bond demonstrate that the enzyme serves not only to stabilize the transition state but also to destabilize the ground state.
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Cyclometalated cluster complex with a butterfly-shaped Pt2Ag2 core.
TL;DR: In solution, the bridging acetone dissociates from the cluster complex 2, but as shown by NMR spectroscopy, the Pt( 2)Ag(2) core is retained in solution and a dynamic equilibrium is suggested to be established between the planar and butterfly skeletal geometries.
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Insights Into the Catalytic Mechanism of Tyrosine Phenol-Lyase from X-Ray Structures of Quinonoid Intermediates.
Dalibor Milić,Tatyana V. Demidkina,Nicolai G. Faleev,Dubravka Matković-Čalogović,Alfred A. Antson +4 more
TL;DR: The mechanism by which binding of the substrate and restructuring of the active site during its closure protect the quinonoid intermediate from the solvent and bring catalytically important residues into positions suitable for the abstraction of phenol during the β-elimination of l-tyrosine is uncovered.