(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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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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M Billeter

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5 October 2019

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A D Kline

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5 October 2019

W Braun

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5 October 2019

R Huber

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5 October 2019

publication date

1 April 1989

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5 October 2019

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11

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Journal of Molecular Biology

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5 October 2019

206

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5 October 2019

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5 October 2019

677-687

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5 October 2019

Conformation of glucagon in a lipid-water interphase by 1H nuclear magnetic resonance

1 reference

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Determination of the complete three-dimensional structure of the alpha-amylase inhibitor tendamistat in aqueous solution by nuclear magnetic resonance and distance geometry

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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

1 reference

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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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Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance

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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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Protein structures in solution by nuclear magnetic resonance and distance geometry. The polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN.

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

1 reference

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

1 reference

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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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Distance geometry and related methods for protein structure determination from NMR data

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

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Comparison of the solution and X-ray structures of barley serine proteinase inhibitor 2.

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Calculation of protein conformations by proton-proton distance constraints. A new efficient algorithm

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

1 reference

9 October 2022

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Identifiers

10.1016/0022-2836(89)90575-5

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:2786963%20AND%20SRC:MED&resulttype=core&format=json

5 October 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:2786963%20AND%20SRC:MED&resulttype=core&format=json

5 October 2019

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