Efforts toward developing probes of protein dynamics: vibrational dephasing and relaxation of carbon-deuterium stretching modes in deuterated leucine.
The spectral position of C-D stretching absorptions in the so-called "transparent window" of protein absorption (1800-2300 cm(-1)) makes them well suited as probes of protein dynamics with high temporal and structural resolution. We have previously incorporated single deuterated amino acids into proteins to site-selectively follow protein folding and ligand binding by steady-state FT IR spectroscopy. Ultimately, our goal is to use C-D bonds as probes in time-resolved IR spectroscopy to study dynamics and intramolecular vibrational energy redistribution (IVR) in proteins. As a step toward this goal, we now present the first time-resolved experiments characterizing the population and dephasing dynamics of selectively excited C-D bonds in a deuterated amino acid. Three differently deuterated, Boc-protected leucines were selected to systematically alter the number of additional C-D bonds that may mediate IVR out of the initially populated bright C-D stretching mode. Three-pulse photon echo experiments show that the steady-state C-D absorption linewidths are broadened by both homogeneous and inhomogeneous effects, and transient grating experiments reveal that IVR occurs on a subpicosecond time scale and is nonstatistical. The results have important implications for the interpretation of steady-state C-D spectra and demonstrate the potential utility of C-D bonds as probes of dynamics and IVR within a protein.
Jörg
J
Zimmermann
Kenan
K
Gundogdu
Matthew E
ME
Cremeens
Jigar N
JN
Bandaria
Gil Tae
GT
Hwang
Megan C
MC
Thielges
Christopher M
CM
Cheatum
Floyd E
FE
Romesberg
D002244:Carbon / Q000737:chemistry*; D003903:Deuterium / Q000737:chemistry*; D007930:Leucine / Q000737:chemistry*; D011506:Proteins / Q000737:chemistry*
D011506:Proteins; D002244:Carbon; D003903:Deuterium; D007930:Leucine