Internal mobility of cyclic RGD hexapeptides studied by 13C NMR relaxation and the model-free approach
Author:
Publisher
Springer Science and Business Media LLC
Subject
Spectroscopy,Biochemistry
Link
http://link.springer.com/content/pdf/10.1007/BF00197634.pdf
Cited by 4 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Exploiting Ligand and Receptor Adaptability in Rational Drug Design Using Dynamics and Structure-Based Strategies;Topics in Current Chemistry;2006
2. Transferred 13C T1 Relaxation at Natural Isotopic Abundance: A Practical Method for Determining Site-Specific Changes in Ligand Flexibility upon Binding to a Macromolecule;Journal of the American Chemical Society;2000-12-01
3. Solution Structure of Substrate-based Ligands When Bound to Hepatitis C Virus NS3 Protease Domain;Journal of Biological Chemistry;1999-06
4. Structure and dynamic properties of the single disulfide-deficient α-amylase inhibitor [C45A/C73A]tendamistat: An NMR study;Proteins: Structure, Function, and Genetics;1998-11-01
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