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High-resolution proton nuclear magnetic resonance studies of protein hydration in aqueous solution show that there are two qualitatively different types of hydration sites. A well-defined, small number of water molecules in the interior of the protein are in identical locations in the crystal structure and in solution, and their residence times are in the range from about 10 -2 to 10 -8 second. Hydration of the protein surface in solution is by water molecules with residence times in the subnanosecond range, even when they are located in hydration sites that contain well-ordered water in the x-ray structures of protein single crystals.
Models, Molecular, Crystallography, Magnetic Resonance Spectroscopy, Protein Conformation, Spectrum Analysis, Proteins, Water, Oxytocin, Solutions, Aprotinin, X-Ray Diffraction, Animals, Cattle, Trypsin Inhibitors, Pancreas
Models, Molecular, Crystallography, Magnetic Resonance Spectroscopy, Protein Conformation, Spectrum Analysis, Proteins, Water, Oxytocin, Solutions, Aprotinin, X-Ray Diffraction, Animals, Cattle, Trypsin Inhibitors, Pancreas
citations This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | 811 | |
popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network. | Top 1% | |
influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | Top 0.1% | |
impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Top 1% |