Gronenborn A - Search Results

1

Analysis of the backbone dynamics of the ribonuclease H domain of the human immunodeficiency virus reverse transcriptase using 15N relaxation measurements.

Powers R, Clore GM, Stahl SJ, Wingfield PT, Gronenborn A. Powers R, et al. Among authors: gronenborn a. Biochemistry. 1992 Sep 29;31(38):9150-7. doi: 10.1021/bi00153a006. Biochemistry. 1992. PMID: 1382587

2

1H and 15N resonance assignments and secondary structure of the human thioredoxin C62A, C69A, C73A mutant.

Forman-Kay JD, Clore GM, Stahl SJ, Gronenborn AM. Forman-Kay JD, et al. Among authors: gronenborn am. J Biomol NMR. 1992 Sep;2(5):431-45. doi: 10.1007/BF02192807. J Biomol NMR. 1992. PMID: 1422155

3

Localization of bound water in the solution structure of the immunoglobulin binding domain of streptococcal protein G. Evidence for solvent-induced helical distortion in solution.

Clore GM, Gronenborn AM. Clore GM, et al. Among authors: gronenborn am. J Mol Biol. 1992 Feb 20;223(4):853-6. doi: 10.1016/0022-2836(92)90247-h. J Mol Biol. 1992. PMID: 1538400

4

Relationship between electrostatics and redox function in human thioredoxin: characterization of pH titration shifts using two-dimensional homo- and heteronuclear NMR.

Forman-Kay JD, Clore GM, Gronenborn AM. Forman-Kay JD, et al. Among authors: gronenborn am. Biochemistry. 1992 Apr 7;31(13):3442-52. doi: 10.1021/bi00128a019. Biochemistry. 1992. PMID: 1554726

In addition, there was no clear evidence that Asp-26 titrates in a manner corresponding to that observed in the Escherichia coli protein [Dyson, H. ...D., Clore, G. M., Wingfield, P. T., & Gronenborn, A. M. (1991) Biochemistry 30, 2685-2698]....

In addition, there was no clear evidence that Asp-26 titrates in a manner corresponding to that observed in the Escherichia coli prot …

5

Three-dimensional solution structure of the E3-binding domain of the dihydrolipoamide succinyltransferase core from the 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coli.

Robien MA, Clore GM, Omichinski JG, Perham RN, Appella E, Sakaguchi K, Gronenborn AM. Robien MA, et al. Among authors: gronenborn am. Biochemistry. 1992 Apr 7;31(13):3463-71. doi: 10.1021/bi00128a021. Biochemistry. 1992. PMID: 1554728

6

High-resolution solution structure of the double Cys2His2 zinc finger from the human enhancer binding protein MBP-1.

Omichinski JG, Clore GM, Robien M, Sakaguchi K, Appella E, Gronenborn AM. Omichinski JG, et al. Among authors: gronenborn am. Biochemistry. 1992 Apr 28;31(16):3907-17. doi: 10.1021/bi00131a004. Biochemistry. 1992. PMID: 1567844

7

1H, 15N, 13C, and 13CO assignments of human interleukin-4 using three-dimensional double- and triple-resonance heteronuclear magnetic resonance spectroscopy.

Powers R, Garrett DS, March CJ, Frieden EA, Gronenborn AM, Clore GM. Powers R, et al. Among authors: gronenborn am. Biochemistry. 1992 May 5;31(17):4334-46. doi: 10.1021/bi00132a026. Biochemistry. 1992. PMID: 1567880

8

Determination of the secondary structure and folding topology of human interleukin-4 using three-dimensional heteronuclear magnetic resonance spectroscopy.

Garrett DS, Powers R, March CJ, Frieden EA, Clore GM, Gronenborn AM. Garrett DS, et al. Among authors: gronenborn am. Biochemistry. 1992 May 5;31(17):4347-53. doi: 10.1021/bi00132a027. Biochemistry. 1992. PMID: 1567881

The secondary structure of human recombinant interleukin-4 (IL-4) has been investigated by three-dimensional (3D) 15N- and 13C-edited nuclear Overhauser (NOE) spectroscopy on the basis of the 1H, 15N, and 13C assignments presented in the preceding paper [Powers, R., Garrett, D. S …

The secondary structure of human recombinant interleukin-4 (IL-4) has been investigated by three-dimensional (3D) 15N- and 13C-edited nuclea …

9

Three-dimensional solution structure of human interleukin-4 by multidimensional heteronuclear magnetic resonance spectroscopy.

Powers R, Garrett DS, March CJ, Frieden EA, Gronenborn AM, Clore GM. Powers R, et al. Among authors: gronenborn am. Science. 1992 Jun 19;256(5064):1673-7. doi: 10.1126/science.256.5064.1673. Science. 1992. PMID: 1609277

10

Stereospecific assignment of beta-methylene protons in larger proteins using 3D 15N-separated Hartmann-Hahn and 13C-separated rotating frame Overhauser spectroscopy.

Clore GM, Bax A, Gronenborn AM. Clore GM, et al. Among authors: gronenborn am. J Biomol NMR. 1991 May;1(1):13-22. doi: 10.1007/BF01874566. J Biomol NMR. 1991. PMID: 1668718

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