The C-terminal domain of human Cdc37 studied by solution NMR

J Biomol NMR. 2015 Nov;63(3):315-21. doi: 10.1007/s10858-015-9988-6. Epub 2015 Sep 24.

Authors

Ziming Zhang¹, Dimitra Keramisanou¹, Amit Dudhat¹, Michael Paré¹, Ioannis Gelis²

Affiliations

¹ Department of Chemistry, University of South Florida, 4202 E. Fowler Ave. CHE 205, Tampa, FL, 33620, USA.
² Department of Chemistry, University of South Florida, 4202 E. Fowler Ave. CHE 205, Tampa, FL, 33620, USA. igelis@usf.edu.

PMID: 26400850
DOI: 10.1007/s10858-015-9988-6

No abstract available

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Cell Cycle Proteins / chemistry*
Chaperonins / chemistry*
Humans
Models, Molecular*
Molecular Sequence Data
Nuclear Magnetic Resonance, Biomolecular* / methods
Protein Conformation*
Protein Interaction Domains and Motifs*
Sequence Alignment
Solutions

Substances

CDC37 protein, human
Cell Cycle Proteins
Solutions
Chaperonins