@article{oai:ir.soken.ac.jp:00004147,
 author = {桑島, 邦博 and KUWAJIMA, Kunihiro and OKAYAMA, Naoki and YAMAMOTO, Kaori and ISHIHARA, Tsuyoshi and SUGAI, Shintaro},
 issue = {1-2},
 journal = {FEBS Letters, FEBS Letters},
 month = {Sep},
 note = {application/pdf, Kinetics of unfolding and refolding of a staphylococcal nuclease mutant, in which Pro117 is replaced by glycine, have been investigated by stopped-flow circular dichroism, and the results are compared with those for the wild-type protein. In contrast to the biphasic unfolding of the wild-type nuclease, the unfolding of the mutant is represented by a single-phase reaction, indicating that the biphasic unfolding for the wild-type protein is caused by cis-trans isomerization about the prolyl peptide bond in the native state. The proline mutation also simplifies the kinetic refolding. Importance of the results in elucidating the folding mechanism is discussed.},
 pages = {135--138},
 title = {The pro117 to glycine mutation of staphylococcal nuclease simplifies the unfolding folding kinetics},
 volume = {290},
 year = {1991}
}