NMR studies of unfolded states of an SH3 domain in aqueous solution and denaturing conditions.
Zhang O, Forman-Kay JD.
Zhang O, et al.
Biochemistry. 1997 Apr 1;36(13):3959-70. doi: 10.1021/bi9627626.
Biochemistry. 1997.
PMID: 9092826
The isolated N-terminal SH3 domain of the Drosophila adapter protein drk (drkN SH3 domain) exists in a dynamic equilibrium between a folded (F(exch)) and an unfolded (U(exch)) state under native-like buffer conditions [Zhang, O., & Forman-Kay, J. D. (1995) Bioch …
The isolated N-terminal SH3 domain of the Drosophila adapter protein drk (drkN SH3 domain) exists in a dynamic equilibrium between a folded …