期刊
BIOMOLECULAR NMR ASSIGNMENTS
卷 13, 期 1, 页码 85-89出版社
SPRINGER
DOI: 10.1007/s12104-018-9857-9
关键词
Pin1; Prolyl isomerase; NMR; Chemical shift assignments; Allostery
资金
- University of Colorado at Denver
Pin1 is a human peptidyl-prolyl cis-trans isomerase important for the regulation of phosphoproteins that are implicated in many diseases including cancer and Alzheimer's. Further biophysical study of Pin1 will elucidate the importance of the two-domain system to regulate its own activity. Here, we report near-complete backbone and side-chain H-1, C-13 and N-15 NMR chemical shift assignments of full-length, apo Pin1 for the purpose of studying interdomain allostery and dynamics.
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