Comparison of the high-resolution structures of the α-amylase inhibitor tendamistat determined by nuclear magnetic resonance in solution and by X-ray diffraction in single crystals

Martin Billeter, Allen D. Kline, Werner Braun, Robert Huber, Kurt Wüthrich

Research output: Contribution to journalArticle

142 Citations (Scopus)

Abstract

The three-dimensional structure of the α-amylase inhibitor Tendamistat determined by nuclear magnetic resonance in aqueous solution is compared with the Tendamistat crystal structure refined at 2·0 Å resolution. Between the two independently obtained structures the root-mean-square distances are 1·05 Å for the backbone atoms N, Cα and C′, 1·25 Å for the backbone and the interior side-chains, and 1·84 Å for all heavy atoms. These numbers show that the interior of the molecule is nearly identical in the two states. Near the protein surface a small number of local differences between the two structures were identified. In most surface areas the solution structure appears more disordered than the crystal structure, with the exception of Tyr15, which was not observed in the X-ray diffraction.

Original languageEnglish (US)
Pages (from-to)677-687
Number of pages11
JournalJournal of Molecular Biology
Volume206
Issue number4
DOIs
StatePublished - Apr 20 1989
Externally publishedYes

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Amylases
X-Ray Diffraction
Magnetic Resonance Spectroscopy
Membrane Proteins
tendamistate

ASJC Scopus subject areas

  • Virology

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Comparison of the high-resolution structures of the α-amylase inhibitor tendamistat determined by nuclear magnetic resonance in solution and by X-ray diffraction in single crystals. / Billeter, Martin; Kline, Allen D.; Braun, Werner; Huber, Robert; Wüthrich, Kurt.

In: Journal of Molecular Biology, Vol. 206, No. 4, 20.04.1989, p. 677-687.

Research output: Contribution to journalArticle

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abstract = "The three-dimensional structure of the α-amylase inhibitor Tendamistat determined by nuclear magnetic resonance in aqueous solution is compared with the Tendamistat crystal structure refined at 2·0 {\AA} resolution. Between the two independently obtained structures the root-mean-square distances are 1·05 {\AA} for the backbone atoms N, Cα and C′, 1·25 {\AA} for the backbone and the interior side-chains, and 1·84 {\AA} for all heavy atoms. These numbers show that the interior of the molecule is nearly identical in the two states. Near the protein surface a small number of local differences between the two structures were identified. In most surface areas the solution structure appears more disordered than the crystal structure, with the exception of Tyr15, which was not observed in the X-ray diffraction.",
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