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Studies by
1
H nuclear magnetic resonance and distance geometry of the solution conformation of the α-amylase inhibitor Tendamistat
Allen D. Kline
,
Werner Braun
, Kurt Wüthrich
Research output
:
Contribution to journal
›
Article
›
peer-review
154
Scopus citations
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Dive into the research topics of 'Studies by
1
H nuclear magnetic resonance and distance geometry of the solution conformation of the α-amylase inhibitor Tendamistat'. Together they form a unique fingerprint.
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Keyphrases
Tendamistat
100%
1H nuclear Magnetic Resonance (1H NMR)
100%
α-amylase Inhibitor
100%
Distance Geometry
100%
Distance Constraint
100%
Solution Conformation
100%
Hydrogen Bonds (H-bonds)
50%
Active Sites
50%
Polypeptide
50%
Nuclear Magnetic Resonance
50%
Side Chain
50%
Disulfide Bridge
50%
Nuclear Overhauser Effect
50%
Bonding Bridge
50%
Hydrogen Disulfide
50%
Angle Constraint
50%
Complete Sequence
50%
Torsion Angle
50%
Sequential Resonance Assignment
50%
Spin-spin Coupling Constants
50%
Biochemistry, Genetics and Molecular Biology
Solution and Solubility
100%
Conformation
100%
Koji
100%
Hydrogen Bond
50%
Active Site
50%
Disulfide
50%
Coupling Constant
50%
Nuclear Overhauser Effect
50%
Resonance Assignment
50%