The remarkable efficiency of a Pin-II proteinase inhibitor sans two conserved disulfide bonds is due to enhanced flexibility and hydrogen bond density in the reactive site loop-Reference-Cited by-同舟云学术

The remarkable efficiency of a Pin-II proteinase inhibitor sans two conserved disulfide bonds is due to enhanced flexibility and hydrogen bond density in the reactive site loop

Published:2012-12-20 Issue:1 Volume:32 Page:13-26
ISSN:0739-1102
Container-title:Journal of Biomolecular Structure and Dynamics
language:en
Short-container-title:Journal of Biomolecular Structure and Dynamics

Author:

Joshi Rakesh S.,Mishra Manasi,Tamhane Vaijayanti A.,Ghosh Anirban,Sonavane Uddhavesh,Suresh C.G.,Joshi Rajendra,Gupta Vidya S.,Giri Ashok P.

Publisher

Informa UK Limited

Subject

Molecular Biology,General Medicine,Structural Biology

Link

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

Reference45 articles.

1. Estimation of Disulfide Bonds Using Ellman’s Reagent

2. Proteins of circularly permuted sequence present within the same organism: The major serine proteinase inhibitor from Capsicum annuum seeds

3. Unbound Form of Tomato Inhibitor-II Reveals Interdomain Flexibility and Conformational Variability in the Reactive Site Loops

4. Structural Basis of Inhibition Revealed by a 1:2 Complex of the Two-headed Tomato Inhibitor-II and Subtilisin Carlsberg

5. Oxidative Folding and Structural Analyses of a Kunitz-Related Inhibitor and Its Disulfide Intermediates: Functional Implications

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