S
Stephen G. Sligar
Researcher at University of Illinois at Urbana–Champaign
Publications - 424
Citations - 37888
Stephen G. Sligar is an academic researcher from University of Illinois at Urbana–Champaign. The author has contributed to research in topics: Cytochrome & Heme. The author has an hindex of 97, co-authored 420 publications receiving 35743 citations. Previous affiliations of Stephen G. Sligar include University of Connecticut Health Center & Sapienza University of Rome.
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Journal ArticleDOI
The energy landscapes and motions of proteins.
TL;DR: The concepts that emerge from studies of the conformational substates and the motions between them permit a quantitative discussion of one simple reaction, the binding of small ligands such as carbon monoxide to myoglobin.
Journal ArticleDOI
Structure and Chemistry of Cytochrome P450
TL;DR: This review will concentrate on findings with P-450cam of the Pseudomonas putida camphor-5-exo-hydroxylase, and attention will be drawn to parallel and contrasting examples from other P- 450s as appropriate.
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Measuring mechanical tension across vinculin reveals regulation of focal adhesion dynamics
Carsten Grashoff,Brenton D. Hoffman,Michael D. Brenner,Ruobo Zhou,Madeline Parsons,Michael T. Yang,Mark A. McLean,Stephen G. Sligar,Christopher S. Chen,Taekjip Ha,Taekjip Ha,Martin A. Schwartz +11 more
TL;DR: Developing a calibrated biosensor that measures forces across specific proteins in cells with piconewton (pN) sensitivity reveals that FA stabilization under force requires both vinculin recruitment and force transmission, and that, surprisingly, these processes can be controlled independently.
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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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Directed self-assembly of monodisperse phospholipid bilayer Nanodiscs with controlled size.
TL;DR: The results of this study provide an important structural characterization of self-assembled phospholipid bilayers and establish a framework for the design of soluble amphiphilic nanoparticles of controlled size.