Single turn peptide alpha helices with exceptional stability in water
| Contribuinte(s) |
Stang, Peter J. |
|---|---|
| Data(s) |
12/02/2005
|
| Resumo |
Cyclic pentapepticles are not known to exist in a-helical conformations. CD and NMR spectra show that specific 20-membered cyclic pentapepticles, Ac-(cyclo-1,5) [KxxxD]-NH2 and Ac-(cyclo-2,6)R[KxxxD]-NH2, are highly a-helical structures in water and independent of concentration, TFE, denaturants, and proteases. These are the smallest a-helical peptides in water. |
| Identificador | |
| Idioma(s) |
eng |
| Publicador |
American Chemical Society |
| Palavras-Chave | #Chemistry, Multidisciplinary #Short Templated Peptides #Ring-closing Metathesis #Solid-phase Synthesis #Protein Secondary Structure #Circular-dichroism Spectra #Side-chain Interactions #Nmr-spectroscopy #Aqueous-solution #Conformational Constraints #Polypeptide Helices #C1 #250301 Organic Chemical Synthesis #780103 Chemical sciences |
| Tipo |
Journal Article |
