Yes if it either A) oligomerizes B) significantly changes shape C) aggregates reversibly
On option B: Lower NaCl could make the protein “appear” bigger by unfolding it a bit; hydrophobic interactions should be weaker in lower NaCl. JPK Artem www.harkerbio.com<http://www.harkerbio.com> "where wild SEC columns roam free" On Jan 11, 2017 7:22 PM, "Reza Khayat" <[email protected]<mailto:[email protected]>> wrote: Hi, Sorry for the off-topic question. Can a protein in lower [NaC] run faster on a SEC than at higher [NaCl] (i.e. elute at an earlier volume)? The protein elutes well within the resolution limits of the SEC with a symmetric gaussian A280 profile. I know that at lower [NaCl] the protein can elute later because it may interact with the matrix. Thanks. Best wishes, Reza Reza Khayat, PhD Assistant Professor City College of New York Department of Chemistry New York, NY 10031
