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William G. Scott
Researcher at University of California, Santa Cruz
Publications - 83
Citations - 28702
William G. Scott is an academic researcher from University of California, Santa Cruz. The author has contributed to research in topics: Ribozyme & Hammerhead ribozyme. The author has an hindex of 40, co-authored 83 publications receiving 24131 citations. Previous affiliations of William G. Scott include Indiana University & University of Minnesota.
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Journal ArticleDOI
Features and development of Coot.
TL;DR: Coot is a molecular-graphics program designed to assist in the building of protein and other macromolecular models and the current state of development and available features are presented.
Journal ArticleDOI
The crystal structure of an all-RNA hammerhead ribozyme: a proposed mechanism for RNA catalytic cleavage.
TL;DR: The crystal structure of an all-RNA hammerhead ribozyme having a single 2'-O-methyl cytosine incorporated at the active site to prevent cleavage has been solved and a mechanism for RNA catalytic cleavage is proposed.
Journal ArticleDOI
Tertiary Contacts Distant from the Active Site Prime a Ribozyme for Catalysis
Monika Martick,William G. Scott +1 more
TL;DR: The full-length hammerhead structure reveals how tertiary interactions occurring remotely from the active site prime this ribozyme for catalysis and permits us to explain the previously irreconcilable sets of experimental results in a unified, consistent, and unambiguous manner.
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Capturing the Structure of a Catalytic RNA Intermediate: The Hammerhead Ribozyme
TL;DR: The crystal structure of an unmodified hammerhead RNA in the absence of divalentMetal ions has been solved, and it was shown that this ribozyme can cleave itself in the crystal when divalent metal ions are added.
Journal ArticleDOI
Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand.
M. V. Milburn,Gilbert G. Privé,Daniel L. Milligan,William G. Scott,Joanne Yeh,Jarmila Jancarik,Daniel E. Koshland,Sung-Hou Kim +7 more
TL;DR: The three-dimensional structure of an active, disulfide cross-linked dimer of the ligand-binding domain of the Salmonella typhimurium as partate receptor and that of an aspartate complex have been determined by x-ray crystallographic methods.