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

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

doi:10.1080/07391102.2013.855144

Cited by 62 publications

(32 citation statements)

References 45 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…MD simulations can track system behavior and understanding of protein folding (Ubaid-Ullah et al 2014;Haque et al 2015;Naiyer et al 2015). These methods are used to investigate the structure, dynamics and thermodynamics of biological molecules (Anwer et al 2015;Hoda et al 2015;Naz et al 2015). In explicit conditions, all atoms of a protein and surrounding water molecules move in a series of time steps.…”

Section: Molecular Dynamic Simulationsmentioning

confidence: 99%

Chitinase from Thermomyces lanuginosus SSBP and its biotechnological applications

et al. 2015

Self Cite

View full text Add to dashboard Cite

Chitinases are ubiquitous class of extracellular enzymes, which have gained attention in the past few years due to their wide biotechnological applications. The effectiveness of conventional insecticides is increasingly compromised by the occurrence of resistance; thus, chitinase offers a potential alternative to the use of chemical fungicides. The thermostable enzymes from thermophilic microorganisms have numerous industrial, medical, environmental and biotechnological applications due to their high stability for temperature and pH. Thermomyces lanuginosus produced a large number of chitinases, of which chitinase I and II are successfully cloned and purified recently. Molecular dynamic simulations revealed that the stability of these enzymes are maintained even at higher temperature. In this review article we have focused on chitinases from different sources, mainly fungal chitinase of T. lanuginosus and its industrial application.

show abstract

Section: Molecular Dynamic Simulationsmentioning

confidence: 99%

Chitinase from Thermomyces lanuginosus SSBP and its biotechnological applications

et al. 2015

Self Cite

View full text Add to dashboard Cite

show abstract

“…The CD spectra of PE stated the intactness and the similarity of present PE with previously reported PE at secondary structural level (Fig. 1b) (Anwer et al 2015). Subunit composition and molecular weight of present PE (Fig.…”

Section: Discussionmentioning

confidence: 86%

“…PE is made up of two peptides, namely, α-and β-subunits containing amino acids ranging from 160 to 180 (Anwer et al 2015;Soni et al 2010). Both the subunits contain covalently attached open chain tetra-pyrrole chromophore/s-the phycoerythrobilin (PEB) (Apt et al 1995).…”

mentioning

confidence: 99%

Phycoerythrin averts intracellular ROS generation and physiological functional decline in eukaryotes under oxidative stress

Sonani

Rastogi

Singh³

et al. 2016

Protoplasma

Self Cite

View full text Add to dashboard Cite

In vitro antioxidant virtue and life-prolonging effect of phycoerythrin (PE; a pigment protein isolated from Phormidium sp. A09DM) have been revealed in our previous reports (Sonani et al. in Age 36:9717, 2014a; Sonani et al. in Process Biochem 49:1757-1766, 2014b). It has been hypothesized that the PE expands life span of Caenorhabditis elegans (bears large resemblance with human aging pathways) due to its antioxidant virtue. This hypothesis is tested in present study by checking the effect of PE on intracellular reactive oxygen species (ROS) generation and associated physiological deformities using mouse and human skin fibroblasts, C. elegans, and Drosophila melanogaster Oregon R and by divulging PE's structural attributes responsible for its antioxidant asset. PE treatment displayed noteworthy decrease of 67, 48, and 77 % in ROS level in mouse fibroblast (3T3-L1), human fibroblast, and C. elegans N2, respectively, arisen under chemical-induced oxidative stress. PE treatment delayed the development of paraquat-induced Alzheimer phenotype by 14.5 % in C. elegans CL4176. Furthermore, PE improved the locomotion of D. melanogaster Oregon R under oxidative stress with simultaneous up-regulation in super-oxide dismutase and catalase activities. The existence of 52 Glu + Asp + His + Thr residues (having metal ion sequestration capacity), 5 phycoerythrobilin chromophores (potential electron exchangers) in PE's primary structure, and significant hydrophobic patches on the surface of its α- and β-subunits are supposed to collectively contribute in the antioxidant virtues of PE. Altogether, results support the hypothesis that it is the PE's antioxidant asset, which is responsible for its life-prolonging effect and thus could be exploited in the therapeutics of ROS-associated abnormalities including aging and neurodegeneration in eukaryotes.

show abstract

“…Biol. Chem., 9 (6): 302-317, 2015 for liquid simulation) in order to investigate its conformational profile Anwer et al, 2015;Stephens et al, 2014;Gramany et al, 2015). Normally, the structure of insulin has two helices.…”

Section: Molecular Dynamics Approachesmentioning

confidence: 99%

From Pancreatic to Non-Pancreatic Insulin: A Miraculous Journey

Anwer¹,

Qumaizi²,

Shaqha³

et al. 2015

International J. of Biological Chemistry

View full text Add to dashboard Cite

The improvement on insulin therapy since it was first administered in early of 20th century is still hunting for better option to cure the metabolic disease the diabetes. Remarkable progress made to date in regard to discovery of peptide hormones like recombinant insulin, insulin analogues, oral insulin and inhaler insulin. But insulin therapy to the patients for long periods resulted in immunological complications due to the development of insulin antibodies that cause insulin allergy and many chronic disorders. Management of diabetes without any side effects is still a challenge to the medical community. Therefore, it is prudent to look for options in herbal medicine. Since its discovery a formidable amount of research, strongly suggest that plants produce a protein with most of the characteristics of vertebrate insulins and plays similar roles in plants as it does in animals. The Molecular Dynamics simulations studies of insulin suggesting an interesting result. It has two constant values at different time scales. This may be due to different chains present in the proteins or different conformations at different time scales of simulation. The relative folding energy of insulin like protein from plant source suggested that it has maximum stability at neutral pH i.e., similar to pH of human blood.

show abstract

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

Cited by 62 publications

References 45 publications

Chitinase from Thermomyces lanuginosus SSBP and its biotechnological applications

Chitinase from Thermomyces lanuginosus SSBP and its biotechnological applications

Phycoerythrin averts intracellular ROS generation and physiological functional decline in eukaryotes under oxidative stress

From Pancreatic to Non-Pancreatic Insulin: A Miraculous Journey

Contact Info

Product

Resources

About