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Loren Dean Williams

Researcher at Georgia Institute of Technology

Publications -  173
Citations -  8442

Loren Dean Williams is an academic researcher from Georgia Institute of Technology. The author has contributed to research in topics: Ribosomal RNA & RNA. The author has an hindex of 49, co-authored 160 publications receiving 7509 citations. Previous affiliations of Loren Dean Williams include University of Mississippi Medical Center & University of Nebraska Medical Center.

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Structural comparison of anticancer drug-DNA complexes: adriamycin and daunomycin.

TL;DR: The observed changes in the overall structures of the ternary complexes amplify the small chemical differences between these two antibiotics and provide a possible explanation for the significantly different clinical activities of these important drugs.
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The B-DNA Dodecamer at High Resolution Reveals a Spine of Water on Sodium†,‡

TL;DR: In this article, a very accurate addition (called structure X here) to the B-DNA dodecamer family of X-ray structures was described, which confirmed the observation of Drew and Dickerson [(1981) J. Mol. Biol. 151, 535−556] that the spine of hydration in AT tract DNA is two layers deep.
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RNA backbone: consensus all-angle conformers and modular string nomenclature (an RNA Ontology Consortium contribution).

TL;DR: A consensus classification and nomenclature are defined for RNA backbone structure using all of the backbone torsion angles and this new backbone system will combine with others that define base pairs, base-stacking, and hydrogen-bond relationships to provide a full description of RNA structural motifs.
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Structure of DNA-porphyrin complex.

TL;DR: In this article, the porphyrin system was shown to be extensively stabilized by electrostatic interactions between positively charged nitrogen atoms of the pyridyl rings and negatively charged phosphate oxygen atoms of DNA.
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X-ray structure of a DNA decamer containing 7,8-dihydro-8-oxoguanine

TL;DR: Additional structural analysis indicates that conversion of G to G(O) would not significantly influence the glycosidic torsion preference of the nucleoside, and the structure allows us to identify probable elements by which the DNA repair protein MutM recognizes its substrates.