ERROR 1
ERROR 1
ERROR 2
ERROR 2
ERROR 2
ERROR 2
ERROR 2
Password and Confirm password must match.
If you have an ACS member number, please enter it here so we can link this account to your membership. (optional)
ERROR 2
ACS values your privacy. By submitting your information, you are gaining access to C&EN and subscribing to our weekly newsletter. We use the information you provide to make your reading experience better, and we will never sell your data to third party members.
Desorption electrospray ionization (DESI) mass spectrometry, a versatile technique for analyzing small molecules, can now be used to analyze proteins and noncovalent protein complexes as large as 150 kilodaltons, chemists report (Anal. Chem., DOI: 10.1021/ac201390w). In conventional DESI, analytes are directly desorbed and ionized from a surface with an electrosprayed solvent. A newer version of DESI for analyzing liquid samples previously extended both the type of samples and the accessible mass range over the original version, but the technique still had not been used for large proteins and protein complexes, until now. Hao Chen of Ohio University, UCLA’s Joseph A. Loo, and coworkers showed that liquid-sample DESI is possible for proteins such as antibodies and noncovalent protein complexes such as manganese superoxide dismutase, a 46-kDa dimeric enzyme, and enolase, a 93-kDa dimeric enzyme. By changing the solvent composition, the researchers can adjust the charge state of the proteins without disrupting their structure and conformation, thus enabling the analysis of larger proteins and protein complexes.
Join the conversation
Contact the reporter
Submit a Letter to the Editor for publication
Engage with us on X