Birdsall B - Search Results

1

Multinuclear NMR characterization of two coexisting conformational states of the Lactobacillus casei dihydrofolate reductase-trimethoprim-NADP+ complex.

Birdsall B, Bevan AW, Pascual C, Roberts GC, Feeney J, Gronenborn A, Clore GM. Birdsall B, et al. Biochemistry. 1984 Sep 25;23(20):4733-42. doi: 10.1021/bi00315a032. Biochemistry. 1984. PMID: 6437442

The complex of Lactobacillus casei dihydrofolate reductase with trimethoprim and NADP+ exists in solution as a mixture of approximately equal amounts of two slowly interconverting conformational states [Gronenborn, A., Birdsall, B., Hyde, E. I., Roberts, G. C. K., F …

The complex of Lactobacillus casei dihydrofolate reductase with trimethoprim and NADP+ exists in solution as a mixture of approximately equa …

2

19 Fnuclear magnetic resonance studies of ligand binding to 3-fluorotyrosine-and 6-fluorotryptophan-containing dihydrofolate reductase from Lactobacillus casei.

Kimber BJ, Griffiths DV, Birdsall B, King RW, Scudder P, Feeney J, Roberts GC, Burgen AS. Kimber BJ, et al. Among authors: birdsall b. Biochemistry. 1977 Jul 26;16(15):3492-500. doi: 10.1021/bi00634a032. Biochemistry. 1977. PMID: 19051 No abstract available.

3

A nuclear magnetic resonance study of nicotinamide adenine dinucleotide phosphate binding to Lactobacillus casei dihydrofolate reductase.

Way JL, Birdsall B, Feeney J, Roberts GC, Burgen AS. Way JL, et al. Among authors: birdsall b. Biochemistry. 1975 Jul 29;14(15):3470-5. doi: 10.1021/bi00686a028. Biochemistry. 1975. PMID: 238594

4

31P-NMR assignment and conformational study of NADPH bound to Lactobacillus casei dihydrofolate reductase based on two-dimensional 1H-31P-heteronuclear and 1H-detected 1H-31P-shift-correlation experiments.

Gerothanassis IP, Birdsall B, Bauer CJ, Feeney J. Gerothanassis IP, et al. Among authors: birdsall b. Eur J Biochem. 1992 Feb 15;204(1):173-7. doi: 10.1111/j.1432-1033.1992.tb16620.x. Eur J Biochem. 1992. PMID: 1740127 Free article.

5

Dihydrofolate reductase: sequential resonance assignments using 2D and 3D NMR and secondary structure determination in solution.

Carr MD, Birdsall B, Frenkiel TA, Bauer CJ, Jimenez-Barbero J, Polshakov VI, McCormick JE, Roberts GC, Feeney J. Carr MD, et al. Among authors: birdsall b. Biochemistry. 1991 Jun 25;30(25):6330-41. doi: 10.1021/bi00239a035. Biochemistry. 1991. PMID: 1905571

6

The 1H-NMR assignments of the aromatic resonances in complexes of Lactobacillus casei dihydrofolate reductase and the origins of their chemical shifts.

Birdsall B, Arnold JR, Jimenez-Barbero J, Frenkiel TA, Bauer CJ, Tendler SJ, Carr MD, Thomas JA, Roberts GC, Feeney J. Birdsall B, et al. Eur J Biochem. 1990 Aug 17;191(3):659-68. doi: 10.1111/j.1432-1033.1990.tb19172.x. Eur J Biochem. 1990. PMID: 2118112 Free article.

7

NMR studies of multiple conformations in complexes of Lactobacillus casei dihydrofolate reductase with analogues of pyrimethamine.

Birdsall B, Tendler SJ, Arnold JR, Feeney J, Griffin RJ, Carr MD, Thomas JA, Roberts GC, Stevens MF. Birdsall B, et al. Biochemistry. 1990 Oct 16;29(41):9660-7. doi: 10.1021/bi00493a022. Biochemistry. 1990. PMID: 2125479

8

NMR studies of differences in the conformations and dynamics of ligand complexes formed with mutant dihydrofolate reductases.

Birdsall B, Andrews J, Ostler G, Tendler SJ, Feeney J, Roberts GC, Davies RW, Cheung HT. Birdsall B, et al. Biochemistry. 1989 Feb 7;28(3):1353-62. doi: 10.1021/bi00429a062. Biochemistry. 1989. PMID: 2496755

9

A kinetic study of wild-type and mutant dihydrofolate reductases from Lactobacillus casei.

Andrews J, Fierke CA, Birdsall B, Ostler G, Feeney J, Roberts GC, Benkovic SJ. Andrews J, et al. Among authors: birdsall b. Biochemistry. 1989 Jul 11;28(14):5743-50. doi: 10.1021/bi00440a007. Biochemistry. 1989. PMID: 2505841

10

Dihydrofolate reductase: multiple conformations and alternative modes of substrate binding.

Birdsall B, Feeney J, Tendler SJ, Hammond SJ, Roberts GC. Birdsall B, et al. Biochemistry. 1989 Mar 7;28(5):2297-305. doi: 10.1021/bi00431a048. Biochemistry. 1989. PMID: 2524214

The complex of Lactobacillus casei dihydrofolate reductase with the substrate folate and the coenzyme NADP+ has been shown to exist in solution as a mixture of three slowly interconverting conformations whose proportions are pH-dependent [Birdsall, B., Gronenborn, A …

The complex of Lactobacillus casei dihydrofolate reductase with the substrate folate and the coenzyme NADP+ has been shown to exist in solut …

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