Abstract
Abstract— The fluorescence spectra of class A proteins which lack tryptophanyl residues were examined in detail, and revealed some differences in the position of maximum and half‐width of the tyrosine emission band between proteins and tyrosine itself. These parameters were affected by conformational changes in protein molecules (denaturation, thermal effects, ion binding) which also induced variations in absorption spectra and fluorescence quantum yields. These observations are thought to be related to the formation of hydrogen bonds between the hydroxyl group of the tyrosyl residues and proton acceptor groups in the protein.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
