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Proton spin-lattice relaxation rate changes induced by freely diffusing oxygen in aqueous and mixed solvents are reported for representative amino acids and glucose. The free energy differences are small, about -800 to -2000 J/mol, but are uniformly negative for all proton positions measured on the amino acids in water and reflect the energetic benefit of weak association of hydrophobic cosolutes.

Research is presented describing the use of nuclear magnetic resonance to measure molecular accessibility to ribonuclease A surface and interior, including amide-hydrogen exchange kinetics, chemical reactivity, nuclear magnetic resonance contact shifts and relaxation, and fluorescence quenching.