insightii biosym (Biosym Technologies)
90
Structured Review
Biosym Technologies
insightii biosym
Insightii Biosym, supplied by Biosym Technologies, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/insightii+biosym/insightii+biosym/pm33779179-334-22-23
Average 90 stars, based on 1 article reviews
Insightii Biosym, supplied by Biosym Technologies, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/insightii+biosym/insightii+biosym/pm33779179-334-22-23
Average 90 stars, based on 1 article reviews
insightii biosym - by Bioz Stars,
2026-09
90/100 stars
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Software:Article Title: Size Dependent Fragmentation Chemistry of Short Doubly Protonated Tryptic Peptides. Article Snippet: Tandem mass spectrometry of electrospray ionized multiply charged peptide ions is commonly used to identify the sequence of peptide(s) and infer the identity of source protein(s).. Doubly protonated peptide ions are consistently the most efficiently sequenced ions following collision-induced dissociation of peptides generated by tryptic digestion.. While the broad characteristics of longer (N ≥ 8 residue) doubly protonated peptides have been investigated, there is comparatively little data on shorter systems where charge repulsion should exhibit the greatest influence on the dissociation chemistry. Article Title: NMR solution structure of type II human cellular retinoic acid binding protein: implications for ligand binding. Article Snippet: The structure of human apo-cellular retinoic acid binding protein II (apo-CRABPII) in solution at pH 7.3 has been determined by NMR spectroscopy.. The sequential assignments of the 1H, 13C, and 15N resonances of apo-CRABPII were established by multinuclear, multidimensional NMR spectroscopy.. The solution structure of apo-CRABPII was derived from 2382 experimental NMR restraints using a hybrid distance geometry-simulated annealing protocol. Article Title: Quantitatively probing propensity for structural transitions in engineered virus nanoparticles by single-molecule mechanical analysis. Article Snippet: View Article Online DOI: 10.1039/C4NR07046A 17 Molecular graphics and structural analyses The programs InsightII ( Article Title: Solution structure of a llama single-domain antibody with hydrophobic residues typical of the VH/VL interface. Article Snippet: The three-dimensional structure of a llama single-domain antibody BrucD4-4 was established by use of solution NMR spectroscopy.. BrucD4-4 has Val, Gly, Leu, and Trp residues at positions 37, 44, 45, and 47, which are considered to be a hallmark to distinguish llama VH from VHH fragments at the germline level.. In contrast to the murine and human VHs, BrucD4-4 has sufficient solubility, is monomeric in solution, and displays high-quality NMR spectra characteristic of well-structured proteins. Article Title: Characterization of the WW domain of human yes-associated protein and its polyproline-containing ligands. Article Snippet: Generated:Article Title: Size Dependent Fragmentation Chemistry of Short Doubly Protonated Tryptic Peptides. Article Snippet: Tandem mass spectrometry of electrospray ionized multiply charged peptide ions is commonly used to identify the sequence of peptide(s) and infer the identity of source protein(s).. Doubly protonated peptide ions are consistently the most efficiently sequenced ions following collision-induced dissociation of peptides generated by tryptic digestion.. While the broad characteristics of longer (N ≥ 8 residue) doubly protonated peptides have been investigated, there is comparatively little data on shorter systems where charge repulsion should exhibit the greatest influence on the dissociation chemistry. Article Title: NMR solution structure of type II human cellular retinoic acid binding protein: implications for ligand binding. Article Snippet: The structure of human apo-cellular retinoic acid binding protein II (apo-CRABPII) in solution at pH 7.3 has been determined by NMR spectroscopy.. The sequential assignments of the 1H, 13C, and 15N resonances of apo-CRABPII were established by multinuclear, multidimensional NMR spectroscopy.. The solution structure of apo-CRABPII was derived from 2382 experimental NMR restraints using a hybrid distance geometry-simulated annealing protocol. Article Title: Quantitatively probing propensity for structural transitions in engineered virus nanoparticles by single-molecule mechanical analysis. Article Snippet: View Article Online DOI: 10.1039/C4NR07046A 17 Molecular graphics and structural analyses The programs InsightII ( Article Title: Solution structure of a llama single-domain antibody with hydrophobic residues typical of the VH/VL interface. Article Snippet: The three-dimensional structure of a llama single-domain antibody BrucD4-4 was established by use of solution NMR spectroscopy.. BrucD4-4 has Val, Gly, Leu, and Trp residues at positions 37, 44, 45, and 47, which are considered to be a hallmark to distinguish llama VH from VHH fragments at the germline level.. In contrast to the murine and human VHs, BrucD4-4 has sufficient solubility, is monomeric in solution, and displays high-quality NMR spectra characteristic of well-structured proteins. Article Title: Characterization of the WW domain of human yes-associated protein and its polyproline-containing ligands. Article Snippet: |