Role of N-terminal residues on folding and stability of C-phycoerythrin: simulation and urea-induced denaturation studies-Reference-Cited by-同舟云学术

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Role of N-terminal residues on folding and stability of C-phycoerythrin: simulation and urea-induced denaturation studies

Published:2013-11-27 Issue:1 Volume:33 Page:121-133
ISSN:0739-1102
Container-title:Journal of Biomolecular Structure and Dynamics
language:en
Short-container-title:Journal of Biomolecular Structure and Dynamics

Author:

Anwer Khalid,Sonani Ravi,Madamwar Datta,Singh Parvesh,Khan Faez,Bisetty Krishna,Ahmad Faizan,Hassan Md. Imtaiyaz

Publisher

Informa UK Limited

Subject

Molecular Biology,General Medicine,Structural Biology

Link

http://www.tandfonline.com/doi/pdf/10.1080/10256018808623883

Reference43 articles.

1. Thermodynamics of the denaturation of lysozyme by guanidine hydrochloride. I. Dependence on pH at 25°

2. Unfolding free energy changes determined by the linear extrapolation method. 2. Incorporation of .DELTA.G.degree.N-U values in a thermodynamic cycle

3. Effects of Guanidine Hydrochloride on the Proton Inventory of Proteins: Implications on Interpretations of Protein Stability

4. The Amber biomolecular simulation programs

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