Site-Specific Protein Dynamics Probed by Ultrafast Infrared Spectroscopy of a Noncanonical Amino Acid
Christopher R Hall, Jinnette Tolentino Collado, James N Iuliano, Agnieszka A Gil, Katrin Adamczyk, Andras Lukacs, Gregory M Greetham, Igor Sazanovich, Peter J Tonge, Stephen R Meech
The Journal of Physical Chemistry B | AMER CHEMICAL SOC | Published : 2019
Real-time observation of structure changes associated with protein function remains a major challenge. Ultrafast pump-probe methods record dynamics in light activated proteins, but the assignment of spectroscopic observables to specific structure changes can be difficult. The BLUF (blue light using flavin) domain proteins are an important class of light sensing flavoprotein. Here, we incorporate the unnatural amino acid (UAA) azidophenylalanine (AzPhe) at key positions in the H-bonding environment of the isoalloxazine chromophore of two BLUF domains, namely, PixD and AppABLUF; both proteins retain the red-shift on irradiation characteristic of photoactivity. Steady state and ultrafast time r..View full abstract
Awarded by EPSRC
Awarded by NSF
S.R.M. is grateful to EPSRC for financial support (EP/N033647/1 and EP/M001997/1). P.J.T. thanks NSF for financial support (CHE-1223819). We gratefully acknowledge STFC for access to the Central Laser Facility.