Contribution of the conserved A16Leu to insulin foldability.
Contributions of the evolutionarily conserved A16Leu and B17Leu to insulin foldability were characterized by evaluating folding properties of single-chain insulin analogs. The results showed A16Leu had much more significant effects on the foldability of insulin than B17Leu.
Zhang
Zhao-Jun
ZJ
Institute of Molecular Biology, College of Life Sciences, Nan Kai University, Tian Jin 300071, China.
Wu
Lan
L
Qiao
Zhi-Song
ZS
Qiao
Ming-Qiang
MQ
Feng
You-Min
YM
Guo
Zhan-Yun
ZY
D000595:Amino Acid Sequence; D000818:Animals; D017124:Conserved Sequence; D004220:Disulfides / Q000737:chemistry; D007328:Insulin / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D007930:Leucine / Q000032:analysis*; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D011384:Proinsulin / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D011487:Protein Conformation; D017510:Protein Folding; D021381:Protein Transport; D013552:Swine
D004220:Disulfides; D007328:Insulin; D011384:Proinsulin; D007930:Leucine