Carbon-13 NMR Studies of Salt Shock-Induced Carbohydrate Turnover in the Marine Cyanobacterium Agmenellum quadruplicatum

Agmenellum quadruplicatum is a unicellular, non-nitrogen-fixing, marine cyanobacterium (blue-green alga). The ultrastructure of this organism, when grown in the laboratory with all necessary nutrients, has been characterized thoroughly. In contrast, little is known of its ultrastructure in the specific nutrient-limiting conditions typical of its natural habitat. Iron is one of the nutrients likely to limit this organism in such natural environments. It is also of great importance metabolically, being required for both photosynthesis and assimilation of nitrate. The purpose of this study was to assess the effects (if any) of iron limitation on the ultrastructure of A. quadruplicatum. It was part of a broader endeavor to elucidate the ultrastructure of cyanobacteria in natural systemsActively growing cells were placed in a growth medium containing 1% of its usual iron. The cultures were then sampled periodically for 10 days and prepared for thin sectioning TEM to assess the effects of iron limitation.

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Metabolism of phenanthrene by the marine cyanobacterium Agmenellum quadruplicatum PR-6.

Applied and Environmental Microbiology ◽

10.1128/aem.58.4.1351-1359.1992 ◽

1992 ◽

Vol 58 (4) ◽

pp. 1351-1359 ◽

Cited By ~ 80

Author(s):

M L Narro ◽

C E Cerniglia ◽

C Van Baalen ◽

D T Gibson

Keyword(s):

Marine Cyanobacterium ◽

Agmenellum Quadruplicatum

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NMR studies of the R2 repeat and related peptide fragments of the DNA binding domain of c-Myb. New light on the structure and folding of R2.

Journal de Chimie Physique ◽

10.1051/jcp:1999235 ◽

1999 ◽

Vol 96 (9/10) ◽

pp. 1580-1584 ◽

Cited By ~ 2

Author(s):

I. Ségalas ◽

S. Desjardins ◽

H. Oulyadi ◽

Y. Prigent ◽

S. Tribouillard ◽

...

Keyword(s):

Dna Binding ◽

Binding Domain ◽

Dna Binding Domain ◽

Peptide Fragments ◽

Nmr Studies ◽

Related Peptide

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2D NMR studies on muscle and cerebral metabolism in vivo

Journal de Chimie Physique ◽

10.1051/jcp/1994910697 ◽

1994 ◽

Vol 91 ◽

pp. 697-703 ◽

Cited By ~ 2

Author(s):

B Gillet ◽

BT Doan ◽

C Verre-Sebrie ◽

O Fedeli ◽

JC Beloeil ◽

...

Keyword(s):

Cerebral Metabolism ◽

2D Nmr ◽

Nmr Studies

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NMR STUDIES OF CONCENTRATED LITHIUM-AMMONIA SOLUTIONS

Le Journal de Physique Colloques ◽

10.1051/jphyscol:1980808 ◽

1980 ◽

Vol 41 (C8) ◽

pp. C8-32-C8-35

Author(s):

Y. Nakamura ◽

M. Niibe ◽

M. Shimoji

Keyword(s):

Nmr Studies

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NMR STUDIES OF Co-BASED NITRIDE AMORPHOUS FILMS

Le Journal de Physique Colloques ◽

10.1051/jphyscol:19888778 ◽

1988 ◽

Vol 49 (C8) ◽

pp. C8-1713-C8-1714

Author(s):

K. Le Dang ◽

P. Veillet ◽

H. Sakakima ◽

R. Krishnan

Keyword(s):

Amorphous Films ◽

Nmr Studies

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Physico-Chemical Properties of Recombinant Desulphatohirudin

Thrombosis and Haemostasis ◽

10.1055/s-0038-1645073 ◽

1990 ◽

Vol 63 (03) ◽

pp. 499-504 ◽

Cited By ~ 4

Author(s):

A Electricwala ◽

L Irons ◽

R Wait ◽

R J G Carr ◽

R J Ling ◽

...

Keyword(s):

Molecular Weight ◽

Gel Filtration ◽

Chemical Properties ◽

Alpha Helix ◽

Apparent Molecular Weight ◽

Correlation Spectroscopy ◽

Nmr Studies ◽

Recombinant Hirudin ◽

Physico Chemical ◽

Recombinant Molecule

SummaryPhysico-chemical properties of recombinant desulphatohirudin expressed in yeast (CIBA GEIGY code No. CGP 39393) were reinvestigated. As previously reported for natural hirudin, the recombinant molecule exhibited abnormal behaviour by gel filtration with an apparent molecular weight greater than that based on the primary structure. However, molecular weight estimation by SDS gel electrophoresis, FAB-mass spectrometry and Photon Correlation Spectroscopy were in agreement with the theoretical molecular weight, with little suggestion of dimer or aggregate formation. Circular dichroism studies of the recombinant molecule show similar spectra at different pH values but are markedly different from that reported by Konno et al. (13) for a natural hirudin-variant. Our CD studies indicate the presence of about 60% beta sheet and the absence of alpha helix in the secondary structure of recombinant hirudin, in agreement with the conformation determined by NMR studies (17)

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NMR studies of alkali intercalted carbon nanotubes

MRS Proceedings ◽

10.1557/proc-772-m3.4 ◽

2003 ◽

Vol 772 ◽

Cited By ~ 1

Author(s):

M. Schmid ◽

C. Goze-Bac ◽

M. Mehring ◽

S. Roth ◽

P. Bernier

Keyword(s):

Carbon Nanotubes ◽

Lattice Relaxation ◽

Spin Lattice Relaxation ◽

Energy Storage Devices ◽

Nmr Studies ◽

Storage Devices ◽

Spin Lattice ◽

Relaxation Measurements ◽

Resonance Spin ◽

Walled Carbon Nanotubes

AbstractLithium intercalted carbon nanotubes have attracted considerable interest as perspective components for energy storage devices. We performed 13C Nuclear Magnetic Resonance spin lattice relaxation measurements in a temperature range from 4 K up to 300 on alkali intercalated Single Walled Carbon Nanotubes in order to investigate the modifications of the electronic properties. The density of states at the Fermi level were determined for pristine, lithium and cesium intercalated carbon nanotubes and are discussed in terms of intercalation and charge transfer effects.

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