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Please use this identifier to cite or link to this item: http://dspace.library.iitb.ac.in/jspui/handle/10054/11537

Title: Zinc-finger hydrolase: Computational selection of a linker and a sequence towards metal activation with a synthetic alpha beta beta protein
Authors: PATEL, K
SRIVASTAVA, KR
DURANI, S
Keywords: secondary structure
chemical-shift
design
nmr
spectroscopy
simulation
assignment
peptides
dynamics
mutants
Issue Date: 2010
Publisher: PERGAMON-ELSEVIER SCIENCE LTD
Citation: BIOORGANIC & MEDICINAL CHEMISTRY, 18(23), 8270-8276
Abstract: The zinc-finger protein is targeted for computational redesign as a hydrolase enzyme. Successful in having zinc activated for hydrolase function, the study validates the stepwise approach to having the protein tuned in main-chain structure stereochemically and over side chains chemically. A leucine homopolypeptide, harboring histidines to tri coordinate zinc and D-amino-acid-nucleated alpha-helix and beta-hairpin building blocks of an alpha beta beta protein, is taken up for modeling, first with CYANA, in a mixed-chirality linker between the building blocks, and then with IDeAS, in a sequence over side chains. The designed mixed-chirality polypeptide structure is proven to order as an intended alpha beta beta fold and capture zinc to activate its role as a hydrolase catalyst. The design approach to have protein folds defined stereochemically and receptor and catalysis functions defined chemically is presented, and illustrates L-and D-alpha-amino-acid structures as the alphabet integrating chemical-and stereochemical-structure variables as its letters.
URI: http://dx.doi.org/10.1016/j.bmc.2010.10.003
http://dspace.library.iitb.ac.in/xmlui/handle/10054/11537
http://hdl.handle.net/10054/11537
ISSN: 0968-0896
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