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David A. Moss

Researcher at Karlsruhe Institute of Technology

Publications -  47
Citations -  1582

David A. Moss is an academic researcher from Karlsruhe Institute of Technology. The author has contributed to research in topics: Beamline & Synchrotron radiation. The author has an hindex of 21, co-authored 47 publications receiving 1510 citations. Previous affiliations of David A. Moss include University of Cambridge & University of Freiburg.

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Redox-linked conformational changes in proteins detected by a combination of infrared spectroscopy and protein electrochemistry. Evaluation of the technique with cytochrome c.

TL;DR: Fourier-transform infrared spectroscopy has been used together with direct electrochemistry of the protein at a modified metal electrode surface and the resulting reduced-minus-oxidized infrared difference spectra show the changes in the frequencies and intensities of molecular vibrations which arise from the redox-linked conformational change.
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Cyclic electron transport in chloroplasts. The Q-cycle and the site of action of antimycin

TL;DR: It is concluded that a Q-cycle can occur in cyclic electron transport with either ferredoxin or 9,10-anthraquinone-2-sulphonate as cofactor; and therefore that the site of action of antimycin in chloroplasts is not within the Q- cycle, as it is believed to be in mitochondria and bacteria.
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Formation of Critical Oligomers Is a Key Event during Conformational Transition of Recombinant Syrian Hamster Prion Protein

TL;DR: Kinetic analysis of the transition process showed that the decrease in α-helical structures and the increase in β-sheet structures occurred concomitantly according to a bimolecular reaction, however, the concentration dependence of the corresponding rate constant pointed to an apparent third order reaction.
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Circulating fibronectin affects bone matrix, whereas osteoblast fibronectin modulates osteoblast function.

TL;DR: It is established that osteoblast‐derived fibronectin solely affects osteoblasts function, and a novel role for liver‐derived circulating fibronsectin thus was defined and delineated from that of locally produced fibronECTin.
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The interactions of duroquinol, dbmib and nqno with the chloroplast cytochrome bf complex

TL;DR: It is proposed that DBMIBH 2 does not form a stable inhibitory complex but can be oxidised by the quinol oxidation site of the cytochrome bf complex, but at a rate which is significantly less than that of oxidation of plastoquinol or duroquinol.