Christopher A. Bottoms, Ph.D.
Affiliations: | 2005 | University of Missouri - Columbia, Columbia, MO, United States |
Area:
Biochemistry, Bioinformatics Biology, Molecular BiologyGoogle:
"Christopher Bottoms"Mean distance: (not calculated yet)
Parents
Sign in to add mentor| John Tanner | grad student | 2005 | University of Missouri - Columbia | |
| (Bioinformatics of protein bound water.) | ||||
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Publications
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| Bottoms CA, Xu D. (2008) Wanted: unique names for unique atom positions. PDB-wide analysis of diastereotopic atom names of small molecules containing diphosphate. Bmc Bioinformatics. 9: S16 |
| Zhou Y, Larson JD, Bottoms CA, et al. (2008) Structural basis of the transcriptional regulation of the proline utilization regulon by multifunctional PutA. Journal of Molecular Biology. 381: 174-88 |
| Ou Z, Bottoms CA, Henzl MT, et al. (2007) Impact of DNA hairpin folding energetics on antibody-ssDNA association. Journal of Molecular Biology. 374: 1029-40 |
| Bottoms CA, White TA, Tanner JJ. (2006) Exploring structurally conserved solvent sites in protein families. Proteins. 64: 404-21 |
| Pattarkine MV, Tanner JJ, Bottoms CA, et al. (2006) Desulfovibrio desulfuricans G20 tetraheme cytochrome structure at 1.5 Angstrom and cytochrome interaction with metal complexes. Journal of Molecular Biology. 358: 1314-27 |
| Beamer LJ, Li X, Bottoms CA, et al. (2005) Conserved solvent and side-chain interactions in the 1.35 Angstrom structure of the Kelch domain of Keap1. Acta Crystallographica. Section D, Biological Crystallography. 61: 1335-42 |
| Bottoms CA, Schuermann JP, Agah S, et al. (2004) Crystal structure of rat alpha-parvalbumin at 1.05 Angstrom resolution. Protein Science : a Publication of the Protein Society. 13: 1724-34 |
| Bottoms CA, Schuermann JP, Agah S, et al. (2004) Crystal Structure of Rat Alpha-Parvalbumin at 1.05 Resolution Protein Science. 13: 1724-1734 |
| Bottoms CA, Smith PE, Tanner JJ. (2002) A structurally conserved water molecule in Rossmann dinucleotide-binding domains. Protein Science : a Publication of the Protein Society. 11: 2125-37 |