PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 12376574-3 2002 In CD(3)OD/D(2)O, 91:9 (v/v), containing 2 mM ammonium acetate, SP-C(Leu) and SP-C exchanged 40% of their exchangeable hydrogens within 1 min. Leucine 69-72 surfactant protein C Homo sapiens 64-68 12376574-7 2002 In contrast, the ion current for SP-C(Leu) was maintained over this time period, although the peptides were incubated together. Leucine 38-41 surfactant protein C Homo sapiens 33-37 10191270-3 1999 However, the folding of synthetic SP-C into an alpha-helix is inefficient and alpha-helical SP-C analogues with Val-->Leu substitutions form oligomers. Leucine 121-124 surfactant protein C Homo sapiens 92-96 11991887-5 2002 The mutation is predicted to substitute a glutamine for a conserved leucine residue and may hinder processing of SP-C precursor protein. Leucine 68-75 surfactant protein C Homo sapiens 113-117 10191270-4 1999 In order to circumvent these problems we have synthesized an SP-C analogue, named SP-C(LKS), which differs from SP-C mainly by the exchange of most of the Val residues in positions 16-28 with Leu residues to promote an alpha-helical conformation, and by the introduction of Lys residues at positions 17, 22 and 27 in order to locate positive charges around the helical circumference and thereby avoid self polymerization. Leucine 192-195 surfactant protein C Homo sapiens 61-65 10191270-4 1999 In order to circumvent these problems we have synthesized an SP-C analogue, named SP-C(LKS), which differs from SP-C mainly by the exchange of most of the Val residues in positions 16-28 with Leu residues to promote an alpha-helical conformation, and by the introduction of Lys residues at positions 17, 22 and 27 in order to locate positive charges around the helical circumference and thereby avoid self polymerization. Leucine 192-195 surfactant protein C Homo sapiens 82-86 10191270-4 1999 In order to circumvent these problems we have synthesized an SP-C analogue, named SP-C(LKS), which differs from SP-C mainly by the exchange of most of the Val residues in positions 16-28 with Leu residues to promote an alpha-helical conformation, and by the introduction of Lys residues at positions 17, 22 and 27 in order to locate positive charges around the helical circumference and thereby avoid self polymerization. Leucine 192-195 surfactant protein C Homo sapiens 82-86