(Q69740387)

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

scientific article published on 01 April 1989

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scholarly article

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5 October 2019

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

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5 October 2019

X-ray diffraction

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K Wüthrich

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5 October 2019

Martin Billeter

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object named as

M Billeter

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5 October 2019

author name string

A D Kline

2

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W Braun

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R Huber

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publication date

1 April 1989

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11

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Journal of Molecular Biology

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206

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677-687

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Solution of the phase problem in the X-ray diffraction method for proteins with the nuclear magnetic resonance solution structure as initial model. Patterson search and refinement for the alpha-amylase inhibitor tendamistat

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Studies by 1H nuclear magnetic resonance and distance geometry of the solution conformation of the alpha-amylase inhibitor tendamistat

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An evaluation of the combined use of nuclear magnetic resonance and distance geometry for the determination of protein conformations in solution

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Gene duplications in the structural evolution of chymotrypsin

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Crystal structure determination, refinement and the molecular model of the alpha-amylase inhibitor Hoe-467A

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Tendamistat (HOE 467), a tight-binding alpha-amylase inhibitor from Streptomyces tendae 4158. Isolation, biochemical properties

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Solution conformation of proteinase inhibitor IIA from bull seminal plasma by 1H nuclear magnetic resonance and distance geometry

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Isolation and structure elucidation of an alpha-amylase inhibitor, AI-3688, from Streptomyces aureofaciens

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Secondary structure of the alpha-amylase polypeptide inhibitor tendamistat from Streptomyces tendae determined in solution by 1H nuclear magnetic resonance

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Identifiers

10.1016/0022-2836(89)90575-5

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5 October 2019

1 reference

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5 October 2019

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