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Reengineering a type II beta-turn as a potential helix nucleator .1. Crystal structure of Boc-Val-Pro-(D)Asp-Asp-Val-OMe monohydrate

DSpace at IIT Bombay

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Title Reengineering a type II beta-turn as a potential helix nucleator .1. Crystal structure of Boc-Val-Pro-(D)Asp-Asp-Val-OMe monohydrate
 
Creator FABIOLA, F
PATTABHI, V
RAJU, EB
DURANI, S
 
Subject peptides
proteins
conformation
 
Description The crystal structure of Boc-Val(1)-Pro(2)-(D)Asp(3)-Asp(4)-Val(5)-OMe is described as a type II beta-turn reengineered into a potential helix nucleator. (D)Asp(3) in the peptide is responsible for the configurationally guided LD chiral type II beta-turn centered at Pro(2)-(D)Asp(3), as well as the partially developed LL chiral type I beta-turn centered at Asp(4)-Val(5) by acceptance of a conformation nucleating H-bond from Val(5)NH to its carboxylic oxygen. (C) Munksgaard 1997.
 
Publisher MUNKSGAARD INT PUBL LTD
 
Date 2011-08-18T21:52:33Z
2011-12-26T12:55:55Z
2011-12-27T05:43:28Z
2011-08-18T21:52:33Z
2011-12-26T12:55:55Z
2011-12-27T05:43:28Z
1997
 
Type Article
 
Identifier JOURNAL OF PEPTIDE RESEARCH, 50(5), 352-356
1397-002X
http://dspace.library.iitb.ac.in/xmlui/handle/10054/10141
http://hdl.handle.net/10054/10141
 
Language en