Protein hydration in aqueous solution

Gottfried Otting; Edvards Liepinsh; Kurt Wüthrich

doi:10.1126/science.1948083

Protein hydration in aqueous solution

Gottfried Otting^*, Edvards Liepinsh, Kurt Wüthrich

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

784 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	974-980
Number of pages	7
Journal	Science
Volume	254
Issue number	5034
DOIs	https://doi.org/10.1126/science.1948083
Publication status	Published - 1991
Externally published	Yes

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abstract = "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.",

author = "Gottfried Otting and Edvards Liepinsh and Kurt W{\"u}thrich",

note = "{\textcopyright} American Association for the Advancement of Science",

year = "1991",

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AU - Otting, Gottfried

AU - Liepinsh, Edvards

AU - Wüthrich, Kurt

N1 - © American Association for the Advancement of Science

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N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/0026326956

U2 - 10.1126/science.1948083

DO - 10.1126/science.1948083

M3 - Article

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SN - 0036-8075

VL - 254

SP - 974

EP - 980

JO - Science

JF - Science

IS - 5034

ER -

Protein hydration in aqueous solution

Abstract

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