D
Daniel P. Bancroft
Researcher at Massachusetts Institute of Technology
Publications - 8
Citations - 1472
Daniel P. Bancroft is an academic researcher from Massachusetts Institute of Technology. The author has contributed to research in topics: Protein structure & DNA. The author has an hindex of 8, co-authored 8 publications receiving 1431 citations. Previous affiliations of Daniel P. Bancroft include University of Utah.
Papers
More filters
Journal ArticleDOI
Crystal structures of the trimeric human immunodeficiency virus type 1 matrix protein : implications for membrane association and assembly
Christopher P. Hill,David K. Worthylake,Daniel P. Bancroft,Allyson M. Christensen,Wesley I. Sundquist +4 more
TL;DR: The crystal structure of the HIV-1 matrix protein, determined at 2.3 angstrom resolution, reveals that individual matrix molecules are composed of five major helices capped by a three-stranded mixed beta-sheet.
Journal ArticleDOI
Platinum-195 NMR kinetic and mechanistic studies of cis- and trans-diamminedichloroplatinum(II) binding to DNA
TL;DR: The kinetics and mechanism of binding of the anticancer drug cis-diamminedichloroplatinum(II), or cis-DDP, and its inactive trans isomer to chicken erythrocyte DNA at 37 o C have been investigated by 195 Pt NMR spectroscopy.
Journal ArticleDOI
Synthesis, characterization, and biological activity of cis-diammineplatinum(II) complexes of the DNA intercalators 9-aminoacridine and chloroquine
TL;DR: The anticancer drug cis-diamminedichloroplatinum (II) reacts with the DNA intercalators 9-aminoacridine (9-AA) and chloroquine (CQ) to form the novel complexes cis-[Pt(NH 3 ) 2 (N9-9AA)Cl](NO 3 ), cis-[Ct( NH 3 )2 (N 9-AA)) 2 ](NO 3 ] 2, and cis[PtNH 3 ), 2(N 1-HCQ)Cl]-NO 3, with the pro
Journal ArticleDOI
Crystal structure of recombinant human platelet factor 4.
TL;DR: The crystal structure of human platelet factor 4 (PF4) has been solved to a resolution of 2.4 A by molecular replacement and refined to an R-factor of 24.1%.
ComponentDOI
The low-temperature crystal structure of the pure-spermine form of Z-DNA reveals binding of a spermine molecule in the minor groove.
TL;DR: The X-ray crystal structure of the pure-spermine form of the left-handed Z-DNA duplex [d(CGCGCG)]2 has been determined and may provide an explanation for the role of spermine as a very effective inducer of the conformational B-DNA to Z- DNA transition with alternating dG-dC sequences in solution.