Search Results - "Düser, Monika G."

Crystal structure of the archaeal A1Ao ATP synthase subunit B from Methanosarcina mazei Gö1: Implications of nucleotide-binding differences in the major A1Ao subunits A and B by Schäfer, Ingmar B, Bailer, Susanne M, Düser, Monika G, Börsch, Michael, Bernal, Ricardo A, Stock, Daniela, Grüber, Gerhard

“…The A1Ao ATP synthase from archaea represents a class of chimeric ATPases/synthases, whose function and general structural design share characteristics both…”
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Elastic deformations of the rotary double motor of single FoF1-ATP synthases detected in real time by Förster resonance energy transfer by Ernst, Stefan, Düser, Monika G., Zarrabi, Nawid, Dunn, Stanley D., Börsch, Michael

“…Elastic conformational changes of the protein backbone are essential for catalytic activities of enzymes. To follow relative movements within the protein,…”
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The Proton-translocating a Subunit of F0F1-ATP Synthase Is Allocated Asymmetrically to the Peripheral Stalk by Düser, Monika G., Bi, Yumin, Zarrabi, Nawid, Dunn, Stanley D., Börsch, Michael

“…The position of the a subunit of the membrane-integral F0 sector of Escherichia coli ATP synthase was investigated by single molecule fluorescence resonance…”
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36° step size of proton-driven c-ring rotation in FoF1-ATP synthase by Düser, Monika G, Zarrabi, Nawid, Cipriano, Daniel J, Ernst, Stefan, Glick, Gary D, Dunn, Stanley D, Börsch, Michael

“…Synthesis of adenosine triphosphate ATP, the ‘biological energy currency’, is accomplished by F o F 1 ‐ATP synthase. In the plasma membrane of Escherichia coli…”
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36 degrees step size of proton-driven c-ring rotation in FoF1-ATP synthase by Düser, Monika G, Zarrabi, Nawid, Cipriano, Daniel J, Ernst, Stefan, Glick, Gary D, Dunn, Stanley D, Börsch, Michael

“…Synthesis of adenosine triphosphate ATP, the 'biological energy currency', is accomplished by F(o)F(1)-ATP synthase. In the plasma membrane of Escherichia…”
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Three-color Förster resonance energy transfer within single F[sub O]F[sub 1]-ATP synthases: monitoring elastic deformations of the rotary double motor in real time by Ernst, Stefan, Düser, Monika G., Zarrabi, Nawid, Börsch, Michael

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The Proton-translocating a Subunit of F0F1-ATP Synthase Is Allocated Asymmetrically to the Peripheral StalkS by Düser, Monika G., Bi, Yumin, Zarrabi, Nawid, Dunn, Stanley D., Börsch, Michael

“…The position of the a subunit of the membrane-integral F 0 sector of Escherichia coli ATP synthase was investigated by single molecule fluorescence resonance…”
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36 degree step size of proton-driven c-ring rotation in FoF1-ATP synthase by Düser, Monika G, Zarrabi, Nawid, Cipriano, Daniel J, Ernst, Stefan, Glick, Gary D, Dunn, Stanley D, Börsch, Michael

“…Synthesis of adenosine triphosphate ATP, the 'biological energy currency', is accomplished by F(o)F(1)-ATP synthase. In the plasma membrane of Escherichia…”
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Simultaneous Monitoring The Two Rotary Motors Of A Single FOF1-ATP Synthase by Düser, Monika G., Zarrabi, Nawid, Ernst, Stefan, Golovina-Leiker, Anastasiya, Reuter, Rolf, Dunn, Stanley D., Börsch, Michael

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Three-color Förster resonance energy transfer within single F₀F₁-ATP synthases: monitoring elastic deformations of the rotary double motor in real time by Ernst, Stefan, Düser, Monika G, Zarrabi, Nawid, Börsch, Michael

“…Catalytic activities of enzymes are associated with elastic conformational changes of the protein backbone. Förster-type resonance energy transfer, commonly…”
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Elastic deformations of the rotary double motor of single F(o)F(1)-ATP synthases detected in real time by Förster resonance energy transfer by Ernst, Stefan, Düser, Monika G, Zarrabi, Nawid, Dunn, Stanley D, Börsch, Michael

“…Elastic conformational changes of the protein backbone are essential for catalytic activities of enzymes. To follow relative movements within the protein,…”
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Crystal Structure of the Archaeal A 1A O ATP Synthase Subunit B from Methanosarcina mazei Gö1: Implications of Nucleotide-binding Differences in the Major A 1A O Subunits A and B by Schäfer, Ingmar B., Bailer, Susanne M., Düser, Monika G., Börsch, Michael, Bernal, Ricardo A., Stock, Daniela, Grüber, Gerhard

“…The A 1A O ATP synthase from archaea represents a class of chimeric ATPases/synthases, whose function and general structural design share characteristics both…”
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Three-color Forster resonance energy transfer within single F sub(O)F sub(1)-ATP synthases: monitoring elastic deformations of the rotary double motor in real time by Ernst, Stefan, Duser, Monika G, Zarrabi, Nawid, Borsch, Michael

“…Catalytic activities of enzymes are associated with elastic conformational changes of the protein backbone. Forster-type resonance energy transfer, commonly…”
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