Abstract
One of the best methods for understanding the forces responsible for holding proteins in their highly cooperative structure is to study effects of amino acid replacements on thermal unfolding of proteins using high sensitivity differential scanning calorimetry (DSC). This article outlines examples of the DSC study on the effects of mutations of T4 phage lysozyme and staphylococcal nuclease.
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.
