Поисковый запрос: (<.>A=Frieden, Carl$<.>) |
Общее количество найденных документов : 11
Показаны документы с 1 по 11
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1.
| Hoeltzli Syndey D. {19}F NMR spectroscopy of [6-{19}F]tryprophan-labeled Escherichia coli dihydrofolate reductase: Equilibrium folding and ligand binding studies // Biochemistry, 1994. Vol. 33, N 18.-С.5502-5509
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| Frieden Intestinal fatty acid binding protein: Folding of fluorescein-modified proteins // Biochemistry, 1995. Vol. 34, N 8.-С.2724-2730
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| Fatty acid interactions with a helix-less variant of intestinal fatty acid-binding protein // Biochemistry, 1996. Vol. 35, N 23.-С.7559-7565
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| Kim Intestinal fatty acid-binding protein: The structure and stability of a helix-less variant // Biochemistry, 1996. Vol. 35, N 23.-С.7553-7558
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| Hoeltzli Sydney D. Refolding of [6-{19}F]tryptophan-labeled Escherichia coli dihydrofolate reductase in the presence of ligand: A stopped-flow NMR spectroscopy study // Biochemistry, 1998. Vol. 37, N 1.-С.387-398
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| Hoeltzli Sydney D. Stopped-flow NMR spectroscopy: Real-time unfolding studies of 6-{19}F-tryptophan-labeled Escherichia coli dihydrofolate reductase // Proc. Nat. Acad. Sci. USA, 1995. Vol. 92, N 20.-С.9318-9322
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7.
| Clark A.Clay Native Escherichia coli and murine dihydrofolate reductases contain late-folding non-native structures // J. Mol. Biol., 1999. Vol. 285, N 4.-С.1765-1776
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| Catalysis of protein folding by chaperones in pathogenic bacteria // Proc. Nat. Acad. Sci. USA, 2004. Vol. 101, N 50.-С.17389-17393
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| Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide // Proc. Nat. Acad. Sci. USA, 2009. Vol. 106, N 48.-С.20324-20329
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| Cortese Microheterogeneity of actin gels formed under controlled linear shear // J. Cell. Biol., 1988. Vol. 107, N 4.-С.1477-1487
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11.
| Frieden Numerical integration of rate equations by computer. An update // Trends Biochem. Sci., 1994. Vol. 18, N 4.-С.181-182
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