Conformational Analysis And Design Of Disulfides In Antiparallel β-Sheets And Helices

Conformational Analysis And Design Of Disulfides In Antiparallel β-Sheets And Helices

Disulfides are the primary covalent interactions within a protein molecule that connect residues which are sequentially distant. Naturally occurring disulfides enhance the stability of the protein by destabilization of the unfolded state. Previous attempts to introduce disulfide bridges as a means...

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Bibliographic Details
Main Author:	Indu, S
Other Authors:	Varadarajan, Raghavan
Language:	en_US
Published:	2013
Subjects:	Protein - Disulphides Helices - Disulfides Antiparallel β-sheets - Disulfides Intrahelical Disulfides Cross-Strand Disulfides Ligand Binding (Biochemistry) - Thermodynamics Molten Globules Protein Stability Disulfide Conformation Biochemistry
Online Access:	http://etd.iisc.ernet.in/handle/2005/2224 http://etd.ncsi.iisc.ernet.in/abstracts/2837/G24433-Abs.pdf

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