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Gramicidin

Known as: Gramicidin [Chemical/Ingredient], Gramicidine, Gramicidins 
A heterogeneous mixture of six antibiotic peptides obtained from the soil bacterium Bacillus brevis. Gramicidin is active against most Gram-positive… Expand
National Institutes of Health

Papers overview

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Highly Cited
2003
Highly Cited
2003
The free energy governing K+ conduction through gramicidin A channels is characterized by using over 0.1 μs of all-atom molecular… Expand
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Highly Cited
2002
Highly Cited
2002
Streptococcus mutans is the leading cause of dental caries (tooth decay) worldwide and is considered to be the most cariogenic of… Expand
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Review
2001
Review
2001
The simplest cell-like structure, the lipid bilayer vesicle, can respond to mechanical deformation by elastic membrane dilation… Expand
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Review
1999
Review
1999
Antimicrobial peptides encompass a wide variety of structural motifs. Many peptides have alpha-helical structures. The majority… Expand
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Highly Cited
1997
Highly Cited
1997
The non-ribosomal synthesis of the cyclic peptide antibiotic gramicidin S is accomplished by two large multifunctional enzymes… Expand
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Highly Cited
1996
Highly Cited
1996
Gramicidin perforated-patch-clamp recordings in brain slices were used to obtain an accurate assessment of the developmental… Expand
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Highly Cited
1995
Highly Cited
1995
The antibiotic gramicidin, when incorporated into lipid membranes, forms pores that are exclusively permeable to monovalent… Expand
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Highly Cited
1993
Highly Cited
1993
The ion channel forming peptide gramicidin A adopts a number of distinct conformations in different environments. We have… Expand
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Highly Cited
1993
Highly Cited
1993
Solid-state nuclear magnetic resonance spectroscopy of uniformly aligned preparations of gramicidin A in lipid bilayers has been… Expand
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Highly Cited
1971
Highly Cited
1971
  • Dan W. Urry
  • Proceedings of the National Academy of Sciences…
  • 1971
  • Corpus ID: 28969048
A lipophilic, left-handed helical structure is proposed for gramicidin A in which the C-O bonds alternately point toward the… Expand
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