Studies by 1H nuclear magnetic resonance and distance geometry of the solution conformation of the α-amylase inhibitor Tendamistat
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Structural Biology
Reference23 articles.
1. Buildup rates of the nuclear Overhauser effect measured by two-dimensional proton magnetic resonance spectroscopy: implications for studies of protein conformation
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3. Die Primärstruktur des α-Amylaseinhibitors Hoe 467A ausStreptomyces tendae4158. Eine neue Klasse von Inhibitoren
4. Interactive program for investigation of protein structures based on 1H NMR experiments
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