Search Results - "Labhardt, Alexander M"

Comprehensive structural and dynamical view of an unfolded protein from the combination of single-molecule FRET, NMR, and SAXS by Aznauryan, Mikayel, Delgado, Leonildo, Soranno, Andrea, Nettels, Daniel, Huang, Jie-rong, Labhardt, Alexander M., Grzesiek, Stephan, Schuler, Benjamin

“…The properties of unfolded proteins are essential both for the mechanisms of protein folding and for the function of the large group of intrinsically…”
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Direct NMR evidence for an intermediate preceding the rate-limiting step in the unfolding of ribonuclease A by Kiefhaber, Thomas, Labhardt, Alexander M, Baldwin, Robert L

“…It is commonly believed that there are no detectable intermediates in the kinetic unfolding reactions of small proteins. If such intermediates could be found,…”
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Template-assembled synthetic proteins with four-helix-bundle topology. Total chemical synthesis and conformational studies by Mutter, Manfred, Tuchscherer, Gabriele G, Miller, Charleen, Altmann, Karl Heinz, Carey, Robert I, Wyss, Daniel F, Labhardt, Alexander M, Rivier, Jean E

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Nature of the fast and slow refolding reactions of iron(III) cytochrome c by Ridge, John A, Baldwin, Robert L, Labhardt, Alexander M

“…The fast and slow refolding reactions of iron(III) cytochrome c (Fe(III) cyt c), previously studied by Ikai et al. (Ikai, A., Fish, W. W., & Tanford, C. (1973)…”
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Proton, carbon-13, and nitrogen-15 NMR backbone assignments and secondary structure of human interferon-.gamma by Grzesiek, Stephan, Doebeli, Heinz, Gentz, Reiner, Garotta, Gianni, Labhardt, Alexander M, Bax, Ad

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A single amino acid substitution in Staphylococcus aureus dihydrofolate reductase determines trimethoprim resistance 1 1 Edited by T.Richmond by Dale, Glenn E., Broger, Clemens, D' Arcy, Allan, Hartman, Peter G., DeHoogt, Ronald, Jolidon, Synèse, Kompis, Ivan, Labhardt, Alexander M., Langen, Hanno, Locher, Hans, Page, Malcolm G.P., Stüber, Dietrich, Then, Rudolf L., Wipf, Beat, Oefner, Christian

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The three-dimensional high resolution structure of human interferon α-2a determined by heteronuclear NMR spectroscopy in solution by Klaus, Werner, Gsell, Bernard, Labhardt, Alexander M., Wipf, Beat, Senn, Hans

“…The solution structure of recombinant human interferon α-2a (Roferon-A) has been determined by multidimensional heteronuclear NMR spectroscopy. The…”
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A single amino acid substitution in Staphylococcus aureus dihydrofolate reductase determines trimethoprim resistance by Dale, G E, Broger, C, D'Arcy, A, Hartman, P G, DeHoogt, R, Jolidon, S, Kompis, I, Labhardt, A M, Langen, H, Locher, H, Page, M G, Stüber, D, Then, R L, Wipf, B, Oefner, C

“…A single amino acid substitution, Phe98 to Tyr98, in dihydrofolate reductase (DHFR) is the molecular origin of trimethoprim (TMP) resistance in Staphylococcus…”
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Measurement of the refolding combination reaction between S-peptide and S-protein by Labhardt, Alexander M, Ridge, John A, Lindquist, Robert N, Baldwin, Robert L

“…S-Peptide combines with S-protein during the refolding of ribonuclease S. The kinetics of combination have now been measured by a specific probe, the…”
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Sequence-specific 1H, 13C and15 N assignment of the TMP-resistant dihydrofolate reductase mutant DHFR(F98Y) in the ternary complex with TMP and NADPH by Altmann, Serge, Labhardt, Alexander M, Senn, Hans, Wüthrich, Kurt

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NMR studies of DNA duplexes singly cross-linked by different synthetic linkers by Altmann, Serge, Labhardt, Alexander M., Bur, Daniel, Lehmann, Christain, Bannwarth, Willi, Billeter, Martin, Wüthrich, Kurt, Leupin, Werner

“…Molecular modelling studies resulted in the design of a variety of non-nucleotidic covalent linkers to bridge the 3′-end of the (+)-strand and the 5′-end of…”
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Secondary structure in ribonuclease. I. Equilibrium folding transitions seen by amide circular dichroism by Labhardt, A M

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A single amino acid substitution in Staphylococcus aureus dihydrofolate reductase determines trimethoprim resistance11Edited by T.Richmond by Dale, Glenn E., Broger, Clemens, D' Arcy, Allan, Hartman, Peter G., DeHoogt, Ronald, Jolidon, Synèse, Kompis, Ivan, Labhardt, Alexander M., Langen, Hanno, Locher, Hans, Page, Malcolm G.P., Stüber, Dietrich, Then, Rudolf L., Wipf, Beat, Oefner, Christian

“…A single amino acid substitution, Phe98 to Tyr98, in dihydrofolate reductase (DHFR) is the molecular origin of trimethoprim (TMP) resistance in Staphylococcus…”
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Secondary structure in ribonuclease. II. Relations between folding kinetics and secondary structure elements by Labhardt, A M

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NMR investigation and secondary structure of domains I and II of rat brain calbindin D 28k (1–93) by Klaus, Werner, Grzesiek, Stephan, Labhardt, Alexander M., Buchwald, Petra, Hunziker, Willi, Gross, Myron D., Kallick, Deborah A.

“…Calbindin D 28k , a member of the troponin C superfamily of calcium‐binding proteins, contains six putative EF hand domains but binds only four calcium‐atoms:…”
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NMR investigation and secondary structure of domains I and II of rat brain calbindin D28k (1–93) by Klaus, Werner, Grzesiek, Stephan, Labhardt, Alexander M., Buchwald, Petra, Hunziker, Willi, Gross, Myron D., Kallick, Deborah A.

“…Calbindin D28k, a member of the troponin C superfamily of calcium‐binding proteins, contains six putative EF hand domains but binds only four calcium‐atoms:…”
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Secondary structure determination for α‐neurotoxin from Dendroaspis polylepis polylepis based on sequence‐specific 1 H‐nuclear‐magnetic‐resonance assignments by LABHARDT, Alexander M., HUNZIKER‐KWIK, Eng‐Hiang, WÜTHRICH, Kurt

“…Sequence‐specific assignments are presented for the polypeptide backbone protons and a majority of the amino‐acid‐side‐chain protons of α‐neurotoxin from…”
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Recombination of S-peptide with S-protein during folding of ribonuclease S. I. Folding pathways of the slow-folding and fast-folding classes of unfolded S-protein by Labhardt, A M, Baldwin, R L

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Recombination of S-peptide with S-protein during folding of ribonuclease S. II. Kinetic characterization of a stable folding intermediate shown by S-protein at pH 1.7 by Labhardt, A M, Baldwin, R L

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Secondary structure determination for α‐neurotoxin from Dendroaspis polylepis polylepis based on sequence‐specific 1H‐nuclear‐magnetic‐resonance assignments by LABHARDT, Alexander M., HUNZIKER‐KWIK, Eng‐Hiang, WÜTHRICH, Kurt

“…Sequence‐specific assignments are presented for the polypeptide backbone protons and a majority of the amino‐acid‐side‐chain protons of α‐neurotoxin from…”
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