Maass G - Search Results

1

Escherichia coli single-stranded DNA binding protein is mobile on DNA: 1H NMR study of its interaction with oligo- and polynucleotides.

Römer R, Schomburg U, Krauss G, Maass G. Römer R, et al. Among authors: maass g. Biochemistry. 1984 Dec 4;23(25):6132-7. doi: 10.1021/bi00320a036. Biochemistry. 1984. PMID: 6395890

2

Escherichia coli single-strand deoxyribonucleic acid binding protein: stability, specificity, and kinetics of complexes with oligonucleotides and deoxyribonucleic acid.

Krauss G, Sindermann H, Schomburg U, Maass G. Krauss G, et al. Among authors: maass g. Biochemistry. 1981 Sep 1;20(18):5346-52. doi: 10.1021/bi00521a040. Biochemistry. 1981. PMID: 7028102

3

Mechanism of discrimination between cognate and non-cognate tRNAs by phenylalanyl-tRNA synthetase from yeast.

Krauss G, Riesner D, Maass G. Krauss G, et al. Among authors: maass g. Eur J Biochem. 1976 Sep;68(1):81-93. doi: 10.1111/j.1432-1033.1976.tb10766.x. Eur J Biochem. 1976. PMID: 9288 Free article.

4

Conformation transitions of a tRNA--aminoacyl-tRNA synthetase complex induced by tRNAs bearing different modifications in the 3' terminus.

Krauss G, von der Haar F, Maass G. Krauss G, et al. Among authors: maass g. Biochemistry. 1979 Oct 16;18(21):4755-61. doi: 10.1021/bi00588a041. Biochemistry. 1979. PMID: 387079

Subtle changes in the 3' terminus are reflected by distinct alterations in the two-step recognition process which had been demonstrated earlier for the native substrate tRNAPheCCA [Krauss, G., Riesner, D., & Maass, G. (1977) Nucleic Acids Res. 4, 2253--22 …

Subtle changes in the 3' terminus are reflected by distinct alterations in the two-step recognition process which had been demonstrated earl …

5

The binding of ethidium bromide to different conformations of tRNA. Unfolding of tertiary structure.

Urbanke C, Römer R, Maass G. Urbanke C, et al. Among authors: maass g. Eur J Biochem. 1973 Mar 15;33(3):511-6. doi: 10.1111/j.1432-1033.1973.tb02710.x. Eur J Biochem. 1973. PMID: 4571499 Free article. No abstract available.

6

Ternary complex formation between elongation factor Tu, GTP and aminoacyl-tRNA: an equilibrium study.

Pingoud A, Urbanke C, Krauss G, Peters F, Maass G. Pingoud A, et al. Among authors: maass g. Eur J Biochem. 1977 Sep;78(2):403-9. doi: 10.1111/j.1432-1033.1977.tb11752.x. Eur J Biochem. 1977. PMID: 334538 Free article.

7

Mechanism of tRNA-aminoacyl-tRNA synthetase recognition: influence of aminoalkyladenylates.

Krauss G, Coutts SM, Riesner D, Maass G. Krauss G, et al. Among authors: maass g. Biochemistry. 1978 Jun 13;17(12):2443-9. doi: 10.1021/bi00605a031. Biochemistry. 1978. PMID: 678524 No abstract available.

8

Tertiary structure of tRNAPhe (yeast): kinetics and electrostatic repulsion.

Urbanke C, Römer R, Maass G. Urbanke C, et al. Among authors: maass g. Eur J Biochem. 1975 Jul 1;55(2):439-44. doi: 10.1111/j.1432-1033.1975.tb02180.x. Eur J Biochem. 1975. PMID: 1104360 Free article.

9

Kinetic study of the three conformational transitions of alanine specific transfer RNA from yeast.

Riesner D, Römer R, Maass G. Riesner D, et al. Among authors: maass g. Eur J Biochem. 1970 Jul;15(1):85-91. doi: 10.1111/j.1432-1033.1970.tb00979.x. Eur J Biochem. 1970. PMID: 5489839 Free article. No abstract available.

10

The coupling of conformational transitions in alanine specific transfer ribonucleic acid from yeast studied by a modified differential absorption technique.

Römer R, Riesner D, Coutts SM, Maass G. Römer R, et al. Among authors: maass g. Eur J Biochem. 1970 Jul;15(1):77-84. doi: 10.1111/j.1432-1033.1970.tb00978.x. Eur J Biochem. 1970. PMID: 5489838 Free article. No abstract available.

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