Suzanne Kiihne, Robert G. Bryant Biophysical Journal

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Protein-Bound Water Molecule Counting by Resolution of 1H Spin-Lattice Relaxation Mechanisms Suzanne Kiihne, Robert G. Bryant Biophysical Journal Volume 78, Issue 4, Pages 2163-2169 (April 2000) DOI: 10.1016/S0006-3495(00)76763-4 Copyright © 2000 The Biophysical Society Terms and Conditions

Figure 1 1H spin-lattice relaxation rate constants for protons in aqueous solutions containing 1% (w/v) BSA at pH*=7.0, and ambient laboratory temperature of 294±1K. (A) The protein was dissolved in D2O and the residual protons measured after equilibration with air. (B) The protein was dissolved in D2O and the residual proton measured after the solution was equilibrated with 1.0atm oxygen gas. (C) The protein was dissolved in D2O and the residual protons measured after the solution was equilibrated with 1.0atm nitrogen gas. (D) The protein was dissolved in H2O and the proton relaxation rate constants measured after the solution was equilibrated with 1.0atm nitrogen gas. The top and bottom axes indicate the electron Larmor frequency and the lower axis indicates the proton Larmor frequency in units of rad/s. Biophysical Journal 2000 78, 2163-2169DOI: (10.1016/S0006-3495(00)76763-4) Copyright © 2000 The Biophysical Society Terms and Conditions