Impact of substrate moisture content on growth and performance of black soldier fly larvae

Experimental data and data analyses growth, respiration and performance of black soldier fly larvae grown at different substrate moisture content

Kirkegaard2017 - 16S rRNA gene amplicon survey of anaerobic digesters

RData file with OTUtables and metadata for a comprehensive survey of anaerobic digester

Calmodulin mutant - F141L apo-form Unstructured C-domain

Assembly members: entity_1, polymer, 148 residues, 16687.334 Da. Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens Experimental source: Production method: recombinant technology Host organism: Escherichia coli Entity Sequences (FASTA): entity_1: ADQLTEEQIAEFKEAFSLFD KDGDGTITTKELGTVMRSLG QNPTEAELQDMINEVDADGN GTIDFPEFLTMMARKMKDTD SEEEIREAFRVFDKDGNGYI SAAELRHVMTNLGEKLTDEE VDEMIREADIDGDGQVNYEE LVQMMTA

Calcium bound form of human calmodulin mutant F141L

Assembly members: entity_1, polymer, 148 residues, 16687.334 Da. entity_CA, non-polymer, 40.078 Da. Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens Experimental source: Production method: recombinant technology Host organism: Escherichia coli Entity Sequences (FASTA): entity_1: ADQLTEEQIAEFKEAFSLFD KDGDGTITTKELGTVMRSLG QNPTEAELQDMINEVDADGN GTIDFPEFLTMMARKMKDTD SEEEIREAFRVFDKDGNGYI SAAELRHVMTNLGEKLTDEE VDEMIREADIDGDGQVNYEE LVQMMTA

2MJR : Anoplin R5W structure in DPC micelles

Experimental Technique/Method:SOLUTION NMR Resolution: Classification:ANTIMICROBIAL PROTEIN Release Date:2014-12-03 Deposition Date:2014-01-16 Revision Date:2015-01-14#2015-01-28 Molecular Weight:24029.57 Macromolecule Type:Protein Residue Count:11 Atom Site Count:1580 DOI:10.2210/pdb2mjr/pdb Abstract: Antimicrobial peptides (AMPs) are promising candidates for battling multiresistant bacteria. Despite extensive research, structure-activity relationships of AMPs are not fully understood, and there is a lack of structural data relating to AMPs in lipids. Here we present the NMR structure of anoplin (GLLKRIKTLL-NH2 ) in a micellar environment. A vast library of substitutions was designed and tested for antimicrobial and hemolytic activity, as well as for changes in structure and lipid interactions. This showed that improvement of antimicrobial activity without concomitant introduction of strong hemolytic activity can be achieved through subtle increases in the hydrophobicity of the hydrophobic face or through subtle increases in the polarity of the hydrophilic face of the helix, or-most efficiently-a combination of both. A set of guidelines based on the results is given, for assistance in how to modify cationic α-helical AMPs in order to control activity and selectivity. The guidelines are finally tested on a different peptide

2MJT : Anoplin R5F T8W in DPC micelles

Experimental Technique/Method:SOLUTION NMR Resolution: Classification:ANTIMICROBIAL PROTEIN Release Date:2014-12-03 Deposition Date:2014-01-16 Revision Date:2015-01-14#2015-01-28 Molecular Weight:24075.64 Macromolecule Type:Protein Residue Count:11 Atom Site Count:1584 DOI:10.2210/pdb2mjt/pdb Abstract: Antimicrobial peptides (AMPs) are promising candidates for battling multiresistant bacteria. Despite extensive research, structure-activity relationships of AMPs are not fully understood, and there is a lack of structural data relating to AMPs in lipids. Here we present the NMR structure of anoplin (GLLKRIKTLL-NH2 ) in a micellar environment. A vast library of substitutions was designed and tested for antimicrobial and hemolytic activity, as well as for changes in structure and lipid interactions. This showed that improvement of antimicrobial activity without concomitant introduction of strong hemolytic activity can be achieved through subtle increases in the hydrophobicity of the hydrophobic face or through subtle increases in the polarity of the hydrophilic face of the helix, or-most efficiently-a combination of both. A set of guidelines based on the results is given, for assistance in how to modify cationic α-helical AMPs in order to control activity and selectivity. The guidelines are finally tested on a different peptide

2MJQ : Structure of antimicrobial peptide anoplin in DPC micelles

Experimental Technique/Method:SOLUTION NMR Resolution: Classification:ANTIMICROBIAL PROTEIN Release Date:2014-12-03 Deposition Date:2014-01-16 Revision Date:2015-01-14#2015-01-28 Molecular Weight:24000.55 Macromolecule Type:Protein Residue Count:11 Atom Site Count:1577 DOI:10.2210/pdb2mjq/pdb Abstract: Antimicrobial peptides (AMPs) are promising candidates for battling multiresistant bacteria. Despite extensive research, structure-activity relationships of AMPs are not fully understood, and there is a lack of structural data relating to AMPs in lipids. Here we present the NMR structure of anoplin (GLLKRIKTLL-NH2 ) in a micellar environment. A vast library of substitutions was designed and tested for antimicrobial and hemolytic activity, as well as for changes in structure and lipid interactions. This showed that improvement of antimicrobial activity without concomitant introduction of strong hemolytic activity can be achieved through subtle increases in the hydrophobicity of the hydrophobic face or through subtle increases in the polarity of the hydrophilic face of the helix, or-most efficiently-a combination of both. A set of guidelines based on the results is given, for assistance in how to modify cationic α-helical AMPs in order to control activity and selectivity. The guidelines are finally tested on a different peptide

2MJS : Anoplin R5K T8W in DPC micelles

Experimental Technique/Method:SOLUTION NMR Resolution: Classification:ANTIMICROBIAL PROTEIN Release Date:2014-12-03 Deposition Date:2014-01-16 Revision Date:2015-01-14#2015-01-28 Molecular Weight:24057.64 Macromolecule Type:Protein Residue Count:11 Atom Site Count:1582 DOI:10.2210/pdb2mjs/pdb Abstract: Antimicrobial peptides (AMPs) are promising candidates for battling multiresistant bacteria. Despite extensive research, structure-activity relationships of AMPs are not fully understood, and there is a lack of structural data relating to AMPs in lipids. Here we present the NMR structure of anoplin (GLLKRIKTLL-NH2 ) in a micellar environment. A vast library of substitutions was designed and tested for antimicrobial and hemolytic activity, as well as for changes in structure and lipid interactions. This showed that improvement of antimicrobial activity without concomitant introduction of strong hemolytic activity can be achieved through subtle increases in the hydrophobicity of the hydrophobic face or through subtle increases in the polarity of the hydrophilic face of the helix, or-most efficiently-a combination of both. A set of guidelines based on the results is given, for assistance in how to modify cationic α-helical AMPs in order to control activity and selectivity. The guidelines are finally tested on a different peptide

2MMJ : Structure of a peptoid analogue of maculatin G15 in DPC micelles

Experimental Technique/Method:SOLUTION NMR Resolution: Classification:ANTIMICROBIAL PROTEIN Release Date:2014-07-23 Deposition Date:2014-03-15 Revision Date:2014-07-30#2014-08-27#2014-12-03 Molecular Weight:2149.58 Macromolecule Type:Protein Residue Count:22 Atom Site Count:153 DOI:10.2210/pdb2mmj/pdb Abstract: The inclusion of peptoid monomers into antimicrobial peptides (AMPs) increases their proteolytic resistance, but introduces conformational flexibility (reduced hydrogen bonding ability and cis/trans isomerism). We here use NMR spectroscopy to answer how the insertion of a peptoid monomer influences the structure of a regular α-helical AMP upon interaction with a dodecyl phosphocholine (DPC) micelle. Insertion of [(2-methylpropyl)amino]acetic acid in maculatin-G15 shows that the structural change and conformational flexibility depends on the site of insertion. This is governed by the micelle interaction of the amphipathic helices flanking the peptoid monomer and the side chain properties of the peptoid and its preceding residue

Additional file 1 of Influence of biofilm growth age, media, antibiotic concentration and exposure time on Staphylococcus aureus and Pseudomonas aeruginosa biofilm removal in vitro

Additional file 1: Figure S1. S. aureus biofilm formation on CBD. After 24 or 72 h of growth, biofilms were removed from the pegs, transferred into the recovery plate and harvested by sonication. Six random wells of each row were selected for CFU count, in total 48 wells per plate. The number of CFUs per peg were different under different conditions. Generally 3 days incubation resulted in more CFUs per peg. Figure S2. P. aeruginosa PA14 biofilm formation on CBD. After 24 or 72 h of growth, biofilms were removed from the pegs, transferred into the recovery plate and harvested by sonication. Six random wells of each row were selected for CFU count, in total 48 wells per plate. The number of CFUs per peg were different under different conditions. Generally 3 days incubation resulted in more CFUs per peg. Figure S3. Flow diagram of the MBEC assay