NMR chemical shift and relaxation measurements provide evidence for the coupled folding and binding of the p53 transactivation domain

The interaction between the acidic transactivation domain of the human tumor suppressor protein p53 (p53TAD) and the 70 kDa subunit of human replication protein A (hRPA70) was investigated using heteronuclear magnetic resonance spectroscopy. A 1H–15N heteronuclear single quantum coherence (HSQC) tit...

Full description

Bibliographic Details
Main Authors: Vise, Pamela D., Baral, Bharat, Latos, Andrew J., Daughdrill, Gary W.
Format: Online
Language:English
Published: Oxford University Press 2005
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1075921/