T
Timothy P. Causgrove
Researcher at Texas A&M University–Corpus Christi
Publications - 27
Citations - 1306
Timothy P. Causgrove is an academic researcher from Texas A&M University–Corpus Christi. The author has contributed to research in topics: Bacteriochlorophyll & Chlorosome. The author has an hindex of 18, co-authored 27 publications receiving 1279 citations. Previous affiliations of Timothy P. Causgrove include Arizona State University & City University of New York.
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Journal ArticleDOI
Fast events in protein folding: helix melting and formation in a small peptide.
Skip Williams,Timothy P. Causgrove,Rudolf Gilmanshin,K S Fang,Robert Callender,W.H. Woodruff,R.B. Dyer +6 more
TL;DR: The observation of the fast kinetics of helix melting in a small 21-residue alanine-based peptide demonstrates that secondary structure formation is fast enough to be a key event at early times in the protein-folding process and that helices are capable of forming before long range tertiary contacts are made.
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Picosecond decay kinetics and quantum yield of fluorescence of the photoactive yellow protein from the halophilic purple phototrophic bacterium, Ectothiorhodospira halophila
TL;DR: The lifetime of the excited state of PYP is remarkably similar to that for the rise of the first photochemical intermediate of bacteriorhodopsin, and underscores the fundamental similarity in their photocycles despite a lack of structural relationship.
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Biochemical characterization and electron-transfer reactions of sym1, a Rhodobacter capsulatus reaction center symmetry mutant which affects the initial electron donor
Aileen K. W. Taguchi,Jonathan W. Stocker,R. G. Alden,Timothy P. Causgrove,Jeffrey M. Peloquin,Steven G. Boxer,Neal W. Woodbury +6 more
TL;DR: Analysis of the sym1 mutant, mutants near P made by other groups, and interspecies variation of amino acids in the vicinity of P suggests that the protein asymmetry in the environment of the initial electron donor is important for optimizing the rate and yield of electron transfer, but is not strictly required for overall reaction center function.
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Redox regulation of energy transfer efficiency in antennas of green photosynthetic bacteria.
Robert E. Blankenship,P. Cheng,Timothy P. Causgrove,Daniel C. Brune,Stephanie Hsiao‐Hsien Wang,Jin‐Ug Choh,Jian Wang +6 more
TL;DR: The results indicate that the energy transfer pathway in green sulfur bacteria is regulated by redox potential, and appears to operate in at least two distinct places, the oligomeric pigments in the interior of the chlorosome and in the bacteriochlorophyll a protein.
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Nonequilibrium protein folding dynamics : laser-induced pH-jump studies of the helix-coil transition
TL;DR: In this article, the helix-coil transition of poly- l -glutamate was measured in the range of 40 ns to 10 ns using a laser-induced pH-jump coupled with time-resolved infrared spectroscopy.