Abstract
NMR has become a method of choice for determining structures of proteins in near-physiological conditions, in particular for dynamic systems. However, in large proteins, line-broadening and spectral overlap often preclude resonance assignment of the many correlation maps needed for structural studies. Various well-described spectroscopic techniques and specific isotopic labeling strategies offer relief from these problems, but it is not always clear which samples should be employed to overcome a particular challenge, nor with which pulse sequences they should be used. Here, we review the challenges associated with assigning large proteins, discuss the many labeling schemes employed to overcome hurdles, and describe associated pulse sequences with focus on both practical concerns and the information content each sequence supplies. Keywords: large protein NMR ; isotopic labeling; protein assignment; backbone resonance assignment; side chain
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.
