Whoa! Big change! Any possible physiological relevance? JPK
From: CCP4 bulletin board [mailto:[email protected]] On Behalf Of Reza Khayat Sent: Wednesday, January 11, 2017 7:43 PM To: [email protected] Subject: Re: [ccp4bb] Off-topic question about SEC All these make sense. Protein is very strange cause it goes from 60kDa (globular) to an apparent 360kDa. Process is reversible too. Reza Khayat, PhD Assistant Professor City College of New York Department of Chemistry New York, NY 10031 ________________________________ From: CCP4 bulletin board <[email protected]<mailto:[email protected]>> on behalf of Keller, Jacob <[email protected]<mailto:[email protected]>> Sent: Wednesday, January 11, 2017 7:39 PM To: [email protected]<mailto:[email protected]> Subject: Re: [ccp4bb] Off-topic question about SEC 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
