Studies of the structure of bacteriophage λ cro protein in solution

Studies of the structure of bacteriophage λ cro protein in solution

“…The two singlets titratable at neutral pH with the chemical shifts of 7.15 and 7.88 ppm (not shown) can be assigned unambiguously to the protons of the C-2 and C-4 in His-35, respectively [12].…”

“…The chemical shifts of signals for only one of the three tyrosines, Tyr II are close to those for free tyrosine or for a tyrosine residue in linear tetrapeptides [ll]; this, however, implies neither its surface location nor its accessibility to a solvent [12].…”

Two‐stage thermal unfolding of [Cys55]‐substituted Cro repressor of bacteriophage λ

“…The protein concentration was measured using the Cro extinction coefficient. A!% = 5.85 [4]. both for Cro and [Cyss5]Cro.…”

An Iterative Fitting Procedure for the Determination of Longitudinal NMR Cross-Correlation Rates

“…Such ratios should allow a valuable estimate of the spectral density functions independent of 15 N CSA tensor values and conformational dynamics (R ex ) relaxation. As described early by Torchia and co-workers (10), R 1 interference effects are much more difficult to measure than R 2 interference rates.…”

“…Recently interest has arisen to also measure R 1 interference effects of CSA and dipolar relaxation, mostly to obtain R 2 /R 1 ratios for the 15 N-1 H CSA-DD cross correlations in proteins. Such ratios should allow a valuable estimate of the spectral density functions independent of 15 N CSA tensor values and conformational dynamics (R ex ) relaxation.…”