Polyproline fold—In imparting kinetic stability to an alkaline serine endopeptidase-Reference-Cited by-同舟云学术

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Polyproline fold—In imparting kinetic stability to an alkaline serine endopeptidase

Published:2013-03 Issue:3 Volume:1834 Page:708-716
ISSN:1570-9639
Container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

Author:

Rohamare Sonali B.,Dixit Vaishali,Nareddy Pavan Kumar,Sivaramakrishna D.,Swamy Musti J.,Gaikwad Sushama M.

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry

Reference55 articles.

1. Protein kinetic stability;Sanchez-Ruiz;Biophys. Chem.,2010

2. Structural basis of protein kinetic stability: resistance to sodium dodecyl sulfate suggests a central role for rigidity and a bias toward β-sheet structure;Manning;Biochemistry,2004

3. Comprehensive analysis of protein folding activation thermodynamics reveals a universal behavior violated by kinetically stable proteases;Jaswal;J. Mol. Biol.,2005

4. Production of alkaline protease from an alkaliphilic actinomycete;Mehta;Bioresour. Technol.,2006

5. Nocardiopsis alkaliphila sp. nov., a novel alkaliphilic actinomycetes isolated from desert soil in Egypt;Hozzein;Int. J. Syst. Evol. Microbiol.,2004

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3. Stability of Alkaline Proteases from Haloalkaliphilic Actinobacteria Probed by Circular Dichroism Spectroscopy;Applied Biochemistry and Microbiology;2018-11

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