Zinc-finger hydrolase: Computational selection of a linker and a sequence towards metal activation with a synthetic alpha beta beta protein

DSpace/Manakin Repository

Zinc-finger hydrolase: Computational selection of a linker and a sequence towards metal activation with a synthetic alpha beta beta protein

Show full item record

Title: Zinc-finger hydrolase: Computational selection of a linker and a sequence towards metal activation with a synthetic alpha beta beta protein
Author: PATEL, K; SRIVASTAVA, KR; DURANI, S
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
Date: 2010


Files in this item

Files Size Format View

There are no files associated with this item.

This item appears in the following Collection(s)

Show full item record

Search DSpace


Advanced Search

Browse

My Account