Thomas Haack scite author profile

The recognition of tetraaspartate peptide (2) by tetra-guanidinium (1) in (a) water and (b) aqueous methanol (10% H2O/90% CH3OH) has been investigated. The conformations of the free peptide and its complex with 1 have been characterized in both solvent systems by CD and 2D NMR spectroscopies. Increased α-helicity as a result of solvent composition and receptor binding are discussed. Control experiments show that the recognition stems from complementary electrostatic interactions, hydrogen bonding, and matching of surface topologies.

show abstract

scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.

Contact Info

customersupport@researchsolutions.com

10624 S. Eastern Ave., Ste. A-614

Henderson, NV 89052, USA

This site is protected by reCAPTCHA and the Google Privacy Policy and Terms of Service apply.

Blog Terms and Conditions API Terms Privacy Policy Contact Cookie Preferences Do Not Sell or Share My Personal Information

Made with 💙 for researchers

Part of the Research Solutions Family.

Thomas Haack

Serine derived oxazolidines as secondary structure disrupting, solubilizing building blocks in peptide synthesis

Recognition and Stabilization of an α-Helical Peptide by a Synthetic Receptor

Phthalazine PDE IV inhibitors: Conformational study of some 6-methoxy-1,4-disubstituted derivatives

Surface Recognition and Helix Stabilization of a Tetraaspartate Peptide by Shape and Electrostatic Complementarity of an Artificial Receptor

Contact Info

Product

Resources

About