Gary W. Daughdrill
Department of Microbiology
Molecular Biology and Biochemistry
University of Idaho
PO Box 443052
USA
Name/email consistency: high
- Dynamic behavior of an intrinsically unstructured linker domain is conserved in the face of negligible amino acid sequence conservation. Daughdrill, G.W., Narayanaswami, P., Gilmore, S.H., Belczyk, A., Brown, C.J. J. Mol. Evol. (2007)
- Reduced spectral density mapping of a partially folded fragment of E. coli thioredoxin. Daughdrill, G.W., Vise, P.D., Zhou, H., Yang, X., Yu, W.F., Tasayco, M.L., Lowry, D.F. J. Biomol. Struct. Dyn. (2004)
- Chemical shift changes provide evidence for overlapping single-stranded DNA- and XPA-binding sites on the 70 kDa subunit of human replication protein A. Daughdrill, G.W., Buchko, G.W., Botuyan, M.V., Arrowsmith, C., Wold, M.S., Kennedy, M.A., Lowry, D.F. Nucleic Acids Res. (2003)
- The weak interdomain coupling observed in the 70 kDa subunit of human replication protein A is unaffected by ssDNA binding. Daughdrill, G.W., Ackerman, J., Isern, N.G., Botuyan, M.V., Arrowsmith, C., Wold, M.S., Lowry, D.F. Nucleic Acids Res. (2001)