Kreutz W - Search Results

1

High resolution 13C-solid state NMR of bacteriorhodopsin: assignment of specific aspartic acids and structural implications of single site mutations.

Engelhard M, Hess B, Metz G, Kreutz W, Siebert F, Soppa J, Oesterhelt D. Engelhard M, et al. Among authors: kreutz w. Eur Biophys J. 1990;18(1):17-24. doi: 10.1007/BF00185416. Eur Biophys J. 1990. PMID: 1968385

2

Magic angle sample spinning 13C nuclear magnetic resonance of isotopically labeled bacteriorhodopsin.

Engelhard M, Hess B, Emeis D, Metz G, Kreutz W, Siebert F. Engelhard M, et al. Among authors: kreutz w. Biochemistry. 1989 May 2;28(9):3967-75. doi: 10.1021/bi00435a051. Biochemistry. 1989. PMID: 2752002

3

Light-driven protonation changes of internal aspartic acids of bacteriorhodopsin: an investigation by static and time-resolved infrared difference spectroscopy using [4-13C]aspartic acid labeled purple membrane.

Engelhard M, Gerwert K, Hess B, Kreutz W, Siebert F. Engelhard M, et al. Among authors: kreutz w. Biochemistry. 1985 Jan 15;24(2):400-7. doi: 10.1021/bi00323a024. Biochemistry. 1985. PMID: 3978081

4

Structural changes of sarcoplasmic reticulum Ca(2+)-ATPase upon Ca2+ binding studied by simultaneous measurement of infrared absorbance changes and changes of intrinsic protein fluorescence.

Georg H, Barth A, Kreutz W, Siebert F, Mäntele W. Georg H, et al. Among authors: kreutz w. Biochim Biophys Acta. 1994 Nov 1;1188(1-2):139-50. doi: 10.1016/0005-2728(94)90032-9. Biochim Biophys Acta. 1994. PMID: 7947901

5

Effect of Triton X-100 and of deuteration on the amplitude of the O640-intermediate in the bacteriorhodopsin photocycle.

Mäntele W, Siebert F, Kreutz W. Mäntele W, et al. Among authors: kreutz w. FEBS Lett. 1981 Jun 15;128(2):249-54. doi: 10.1016/0014-5793(81)80092-0. FEBS Lett. 1981. PMID: 7262318 Free article. No abstract available.

6

Flash-induced kinetic infrared spectroscopy applied to biochemical systems.

Siebert F, Mäntele W, Kreutz W. Siebert F, et al. Among authors: kreutz w. Biophys Struct Mech. 1980;6(2):139-46. doi: 10.1007/BF00535750. Biophys Struct Mech. 1980. PMID: 7388122

7

Two distinct rhodopsin molecules within the disc membrane of vertebrate rod outer segments.

Hoffmann W, Siebert F, Hofmann KP, Kreutz W. Hoffmann W, et al. Among authors: kreutz w. Biochim Biophys Acta. 1978 Sep 7;503(3):450-61. doi: 10.1016/0005-2728(78)90144-5. Biochim Biophys Acta. 1978. PMID: 28757

8

Molecular changes in the sarcoplasmic reticulum calcium ATPase during catalytic activity. A Fourier transform infrared (FTIR) study using photolysis of caged ATP to trigger the reaction cycle.

Barth A, Kreutz W, Mäntele W. Barth A, et al. Among authors: kreutz w. FEBS Lett. 1990 Dec 17;277(1-2):147-50. doi: 10.1016/0014-5793(90)80830-c. FEBS Lett. 1990. PMID: 2148528 Free article.

9

Protonation of Glu L212 following QB- formation in the photosynthetic reaction center of Rhodobacter sphaeroides: evidence from time-resolved infrared spectroscopy.

Hienerwadel R, Grzybek S, Fogel C, Kreutz W, Okamura MY, Paddock ML, Breton J, Nabedryk E, Mäntele W. Hienerwadel R, et al. Among authors: kreutz w. Biochemistry. 1995 Mar 7;34(9):2832-43. doi: 10.1021/bi00009a013. Biochemistry. 1995. PMID: 7893696

10

Changes of protein structure, nucleotide microenvironment, and Ca(2+)-binding states in the catalytic cycle of sarcoplasmic reticulum Ca(2+)-ATPase: investigation of nucleotide binding, phosphorylation and phosphoenzyme conversion by FTIR difference spectroscopy.

Barth A, Kreutz W, Mäntele W. Barth A, et al. Among authors: kreutz w. Biochim Biophys Acta. 1994 Aug 24;1194(1):75-91. doi: 10.1016/0005-2736(94)90205-4. Biochim Biophys Acta. 1994. PMID: 8075144

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