René Jules Dubos

Moberg, Carol L.; Cohn, Zanvil A.

doi:10.1038/scientificamerican0591-66

Cited by 21 publications

(12 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The linear peptide gramicidin A (GA) has been extensively used to study the organization, dynamics, and function of membrane-spanning channels so far [1,3,4,[7][8][9][10][11][12]. The GA is produced by the soil bacterium and consists of alternating L-and D-amino acids [7].…”

Section: Introductionmentioning

confidence: 99%

Molecular dynamics studies of lipid bilayer with gramicidin A: Effects of gramicidin a on membrane structure and hydrophobic match

Saito

Mizukami

Kawamoto

et al. 2011

Int J of Quantum Chemistry

View full text Add to dashboard Cite

The effects of gramicidin A (GA) peptide on the structure of lipid bilayer were studied by molecular dynamics (MD) simulations in the absence and presence of GA peptide. The hydrophobic match between the GA and surrounding lipid bilayer was investigated by the MD simulations of four kinds of lipid bilayer systems: 1,2-dilauroyl-sn-glycero-3-phosphatidylcholine (diC12:0-PC), 1,2-dimyristoyl-sn-glycero-3-phosphatidylcholine (DMPC, diC14:0-PC), 1,2-dipalmitoyl-sn-glycero-3-phosphatidylcholine (diC16:0-PC), and 1,2-distearoyl-sn-glycero-3-phosphatidylcholine (DSPC, di18:0-PC). The observed hydrophobic thickness and order parameter increases, and the gauche conformation decreases in the presence of GA, being consistent with the experimental observations. The acyl chain structure of the DSPC membrane was sufficiently changed to match the length of GA peptide, resulting in a distortion of the membrane surface around the GA peptide. On the other hand, the minor structural changes of lipid and the small fluctuation of the GA were shown in the DMPC membrane. These results Additional Supporting Information may be found in the online version of this article. indicate that DMPC bilayer has a better hydrophobic match with the GA peptide than the other membranes.

show abstract

Section: Introductionmentioning

confidence: 99%

Molecular dynamics studies of lipid bilayer with gramicidin A: Effects of gramicidin a on membrane structure and hydrophobic match

Saito

Mizukami

Kawamoto

et al. 2011

Int J of Quantum Chemistry

View full text Add to dashboard Cite

show abstract

“…Gramicidin is an antibacterial peptide that forms ion channels specific for monovalent cations in the membrane 1. The organization, dynamics, and function of linear peptide gramicidin A (GA) has been studied so far 1–9. As the side chain orientations of gramicidin tryptophan residues play an important role in channel activity, the special emphasis has been given to the role and orientation of tryptophan residues in channel structure 8.…”

Section: Introductionmentioning

confidence: 99%

Racial disparities and treatment trends in a large cohort of elderly black and white patients with nonsmall cell lung cancer

Hardy

Liu

Xia

et al. 2009

Cancer

121

View full text Add to dashboard Cite

A series of new semiconducting polymers based on 4,4‐dihexyl‐4H‐cyclopenta[2,1‐b:3,4‐b′]dithiophene, 2,2‐dihexyl‐2H‐benzimidazole, and thiophene units was synthesized. The polymers show good solubility at room temperature in organic solvents owing to long alkyl chain in new acceptor, 2,2‐dihexyl‐2H‐benzimidazole. The advantage of dihexyl‐2H‐benzimidazole compared to the benzothiadiazole is to improve the solubility of the polymer. It was found that these polymers can finely be tuned for photovoltaic application by adjusting the contents ratio of the dihexyl‐2H‐benzimidazole unit. The spectra of the solid films show absorption bands with maximum peaks in the range of 421–577 nm and the absorption onsets at 588–683 nm, corresponding to band gaps of 2.11–1.82 eV. The devices with PCPDTDTHBI‐1:PC71BM showed an open‐circuit voltage (VOC) of 0.46 V, a short‐circuit current density (JSC) of 3.83 mA/cm2, and a fill factor of 0.36, giving a power conversion efficiency of 0.64%. Decrease of the dihexyl‐2H‐benzimidazole contents in the polymers induced red‐shift of the UV absorptions, and increased VOC and JSC values, to improve the efficiency of organic photovoltaics. © 2010 Wiley Periodicals, Inc. J Polym Sci Part A: Polym Chem, 2010

show abstract

“…The capsule surrounding the pneumococcus was, like cellulose, a polysaccharide. Using the soil enrichments from a New Jersey cranberry bog, Dubos isolated an enzyme that destroyed the capsule and rendered the pathogen susceptible to phagocytosis by white blood cells (Moberg, 2005; Moberg and Cohn, 1991).…”

Section: Soil Scientists In the Larger Scientific World: Vernadsky Dmentioning

confidence: 99%

Hooked! Seductive Details in Soil Science

Landa

2015

Soil Horizons

View full text Add to dashboard Cite

René Jules Dubos

Cited by 21 publications

References 0 publications

Molecular dynamics studies of lipid bilayer with gramicidin A: Effects of gramicidin a on membrane structure and hydrophobic match

Molecular dynamics studies of lipid bilayer with gramicidin A: Effects of gramicidin a on membrane structure and hydrophobic match

Racial disparities and treatment trends in a large cohort of elderly black and white patients with nonsmall cell lung cancer

Hooked! Seductive Details in Soil Science

Contact Info

Product

Resources

About