Trinitromethanide and Tricyanomethanide Salts Restricted to C, H, N, and 0 Atoms

Gunasekaran, A.; Boyer, J. H.

doi:10.21236/ada254523

Cited by 3 publications

(3 citation statements)

References 6 publications

(9 reference statements)

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“…The bis-diazonium salt of the diamine 7 was converted to diazidoazofurazan 8 On the other hand, nitrogen evolution was thwarted by distillation when attempts were made to bring about thermal decomposition of the neat azide 5, bp 165°C. Although the azide 4 in inert solvents underwent both thermolysis and photolysis to give dibenzo-l,3a,4,6a-tetraazapentalene 10 [6], similar experiments with the azide 5 gave unidentified and intractable material without the detection of either difurazano-l,3a,4,6atetraazapentalene 11 or the isomeric difurazano-1,2,5,6-tetraazacyclooctatetraene 12 [lo].…”

Section: Results and Discusszonmentioning

confidence: 99%

Dense energetic compounds of C, H, N, and O atoms IV nitro and azidofurazan derivatives

Gunasekaran

Trudell

Boyer

1994

Heteroatom Chemistry

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Section: Results and Discusszonmentioning

confidence: 99%

Dense energetic compounds of C, H, N, and O atoms IV nitro and azidofurazan derivatives

Gunasekaran

Trudell

Boyer

1994

Heteroatom Chemistry

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“…[46] Researches involved in peptide and protein design have exploited the conformational properties of Pro to analyze and realize an array of secondary structural features. [47][48][49] The statistics of the individual geometric parameters for every canonical amino acid residue are summarized in Figure 2. The box plots reveal that torsions ψ and χ have a large variation in means, presumably because they have a very wide range of accessible conformations.…”

Section: Counts and Descriptive Statistics Of Canonical Residuesmentioning

confidence: 99%

Analysis of residue conformations in peptides in Cambridge structural database and protein‐peptide structural complexes

Raghavender

2016

Chem Biol Drug Des

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A comprehensive statistical analysis of the geometric parameters of peptide chains in a reduced dataset of protein-peptide complexes in Protein Data Bank (PDB) is presented. The angular variables describing the backbone conformations of amino acid residues in peptide chains shed insights into the conformational preferences of peptide residues interacting with protein partners. Nonparametric statistical approaches are employed to evaluate the interrelationships and associations in structural variables. Grouping of residues based on their structure into chemical classes reveals characteristic trends in parameter relationships. A comparison of canonical amino acid residues in free peptide structures in Cambridge structural database (CSD) with identical residues in PDB complexes, suggests that the information can be integrated from both the structural repositories enabling efficient and accurate modeling of biologically active peptides.

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“…3 As in p-helix, the p-turn would encompass the largest space relative to smaller member b-and a-turns and there is the possibility of water molecules being entrapped in the space. Indeed, the Schellman motif, 4 which is a special case of p-turn occurring at the C-termini of helices, has been reported to contain such water molecules, 5 although a detailed analysis is still lacking. There are other locations in tertiary structures where classical p-turns with a hydrogen bond between the CO and NH groups of residues (i) and (i 1 5) are also observed.…”

Section: Introductionmentioning

confidence: 99%

Water and side‐chain embedded π‐turns

2014

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Elucidating protein function from its structure is central to the understanding of cellular mechanisms. This involves deciphering the dependence of local structural motifs on sequence. These structural motifs may be stabilized by direct or water-mediated hydrogen bonding among the constituent residues. π-Turns, defined by interactions between (i) and (i + 5) positions, are large enough to contain a central space that can embed a water molecule (or a protein moiety) to form a stable structure. This work is an analysis of such embedded π-turns using a nonredundant dataset of protein structures. A total of 2965 embedded π-turns have been identified, as also 281 embedded Schellman motif, a type of π-turn which occurs at the C-termini of α-helices. Embedded π-turns and Schellman motifs have been classified on the basis of the protein atoms of the terminal turn residues that are linked by the embedded moiety, conformation, residue composition, and compared with the turns that have terminal residues connected by direct hydrogen bonds. Geometrically, the turns have been fitted to a circle and the position of the linker relative to its center analyzed. The hydroxyl group of Ser and Thr, located at (i + 3) position, is the most prominent linker for the side-chain mediated π-turns. Consideration of residue conservation among homologous sequences indicates the terminal and the linker positions to be the most conserved. The embedded π-turn as a binding site (for the linker) is discussed in the context of "nest," a concave depression that is formed in protein structures with adjacent residues having enantiomeric main-chain conformations.

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Trinitromethanide and Tricyanomethanide Salts Restricted to C, H, N, and 0 Atoms

Cited by 3 publications

References 6 publications

Dense energetic compounds of C, H, N, and O atoms IV nitro and azidofurazan derivatives

Dense energetic compounds of C, H, N, and O atoms IV nitro and azidofurazan derivatives

Analysis of residue conformations in peptides in Cambridge structural database and protein‐peptide structural complexes

Water and side‐chain embedded π‐turns

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