PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2789994-7 1989 A wobble alignment of the O6alkG4.C9 base pair stablized by two hydrogen bonds, one between the amino group of C9 and N1 of O6alkG and the other between the amino group of O6alkG and N3 of C9, is tentatively proposed on the basis of the NOEs between the amino protons of C9 at the lesion site and the imino protons of flanking Watson-Crick base pairs. Hydrogen 64-72 complement C9 Homo sapiens 111-130 2372316-18 1990 The few NOE crosspeaks, pH dependence, and Cu2+ broadening of C9 1H signals indicate an isolated location accessible to solvent. Hydrogen 65-67 complement C9 Homo sapiens 62-64 8652545-6 1996 The energetic cost of removal of hydroxyl groups at the C-9 and C-14 positions (which structural studies indicate may participate in hydrogen-bonding interactions with the DNA) was approximately 1 kcal mol(-1). Hydrogen 133-141 complement C9 Homo sapiens 56-59 26400077-1 2015 The de novo design of a beta/gamma-peptidic foldamer motif has led to the discovery of an unprecedented 9/8-ribbon featuring an uninterrupted alternating C9/C8 hydrogen-bonding network. Hydrogen 160-168 complement C9 Homo sapiens 154-159 5639923-5 1968 The location of five of the six labelled hydrogen atoms at C-3, C-9, C-18 and C-19 (two) confirms that the mechanism of cyclization of squalene expected from the biogenetic isoprene rule is functioning in vivo. Hydrogen 41-49 complement C9 Homo sapiens 64-67 20564041-6 2010 The Gpn residue can adopt both C(7) (NH(i) CO(i)) and C(9) (CO(i-1) NH(i+1)) hydrogen bonds which are analogous to the C(5) and C(7) (gamma-turn) conformations at alpha-residues. Hydrogen 77-85 complement C9 Homo sapiens 54-58 24625033-6 2014 By comparing the oxysterol profile formed from 7-DHC and those formed from 8-DHC and 5,8(14)-dienol, products formed from abstraction of the hydrogen atoms at C-9 and C-14 (H-9 or H-14 mechanism) were clearly differentiated. Hydrogen 141-149 complement C9 Homo sapiens 159-162