Zobrazeno 1 - 10
of 77
pro vyhledávání: '"Mary D. Barkley"'
Publikováno v:
The Journal of Physical Chemistry B. 115:3245-3253
Tryptophan (Trp) fluorescence is potentially a powerful probe for studying the conformational ensembles of proteins in solution, as it is highly sensitive to the local electrostatic environment of the indole side chain. However, interpretation of the
Publikováno v:
Biophysical Journal. 100:144-153
Efavirenz is a second-generation nonnucleoside reverse transcriptase inhibitor (NNRTI) and a common component of clinically approved anti-AIDS regimens. NNRTIs are noncompetitive inhibitors that bind in a hydrophobic pocket in the p66 subunit of reve
Publikováno v:
Biochemistry. 48:7646-7655
Crystal structures and simulations suggest that conformational changes are critical for the function of HIV-1 reverse transcriptase. The enzyme is an asymmetric heterodimer of two subunits, p66 and p51. The two subunits have the same N-terminal seque
Publikováno v:
The Journal of Physical Chemistry B. 110:7009-7016
The wavelength of maximum emission of tryptophan depends on the local electrostatic environment of the indole chromophore. The time-resolved emission spectra of seven rigid cyclic hexapeptides containing a single tryptophan residue were measured. The
Autor:
Chia Pin Pan, Mary D. Barkley
Publikováno v:
Biophysical Journal. 86:3828-3835
The peptide bond quenches tryptophan fluorescence by excited-state electron transfer, which probably accounts for most of the variation in fluorescence intensity of peptides and proteins. A series of seven peptides was designed with a single tryptoph
Autor:
Mark L. McLaughlin, Frank R. Fronczek, Reema K. Thalji, Mary D. Barkley, Bo Liu, Paul D. Adams
Publikováno v:
Journal of the American Chemical Society. 124:13329-13338
A constrained derivative, cis-1-amino-2-(3-indolyl)cyclohexane-1-carboxylic acid, cis-W3, was designed to test the rotamer model of tryptophan photophysics. The conformational constraint enforces a single chi(1) conformation, analogous to the chi(1)
Publikováno v:
Biochemistry. 40:12140-12149
The central termination sequence (CTS) terminates (+) strand DNA synthesis in certain lentiviruses. The molecular mechanism underlying this event, catalyzed by equine infectious anemia virus reverse transcriptase (EIAV RT), was evaluated by pre-stead
Publikováno v:
The Journal of Physical Chemistry B. 104:1837-1843
Tryptophan analogues with unique spectral and photophysical properties offer intrinsic fluorescent probes for studying peptide−protein and protein−protein interactions. Two benzannulated indole derivatives, benz[f]indole and 3-methylbenz[f]indole
Autor:
Guillermo A. Morales, Mark L. McLaughlin, Mary D. Barkley, Frank R. Fronczek, Lloyd P. McMahon, Marco A. Vela, Hongtao Yu, Li Shui
Publikováno v:
The Journal of Physical Chemistry B. 101:3269-3280
The conformer model of tryptophan photophysics ascribes the multiple fluorescence lifetimes to ground-state heterogeneity. It is usually assumed that the different conformers do not interconvert in the excited state. Previous studies of two constrain
Publikováno v:
Biophysical Journal. 70(4):1923-1932
Tomaymycin reacts covalently with guanine in the DNA minor groove, exhibiting considerable specificity for the flanking bases. The sequence dependence of tomaymycin bonding to DNA was investigated in synthetic DNA oligomers and polymers. The maximum