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Chain conformation in polyretropeptides III: Design of a 310 helix using a,a-dialkylated amino acids and retropeptide bonds

Autor
Aleman, C.
Tipus d'activitat
Article en revista
Revista
Proteins
Data de publicació
1997-01-01
Volum
29
Número
4
Pàgina inicial
575
Pàgina final
582
DOI
10.1002/(SICI)1097-0134(199712)29:4<575::AID-PROT16>3.0.CO;2-J
URL
http://onlinelibrary.wiley.com/doi/10.1002/(SICI)1097-0134(199712)29:4%3C575::AID-PROT16%3E3.0.CO;2-J/abstract;jsessionid=1CB813511FCD2306E395A704B6073808.f01t03 Obrir en finestra nova
Resum
Computer simulations have been used to design a polypeptide with a 310 helix conformation. The study has been been performed taking advantage of the intrinsic helix forming tendency of a-Aminoisobutyric acid. In order to avoid the formation of the a helix, which is the other common helical conformation adopted by a-Aminoisobutyric acid-based peptides, retropeptide bonds have been included in the sequence. Thus, retropeptides are not able to form the intramolecular hydrogen bonding interactions c...
Paraules clau
310 helix, Polypeptides, rAib residue
Grup de recerca
CRnE - Centre de Recerca en Ciència i Enginyeria Multiescala de Barcelona
IMEM-BRT- Innovation in Materials and Molecular Engineering - Biomaterials for Regenerative Therapies

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