Study of Solvent Accessible Regions , Hydrophobicity and Antigenicity of NADH
نویسنده
چکیده
Sonu Mishra1 and Virendra S. Gomase2 1,2Department of Biotechnology, MewarUniversity, Chittorgarh, India, *E-mail – [email protected], [email protected] Department of Biotechnology, MewarUniversity, Chittorgarh, India *Corresponding Author: Sonu Mishra, Department of Biotechnology, MewarUniversity, Chittorgarh, India Email: sonumishra1014@ gmail.com Citation: Sonu Mishra et.al (2016). Study of Solvent Accessible Regions ,Hydrophobicity and Antigenicity of NADH dehydrogenase subunit 3 Int J Vac & Im Sys. 1:1 7-13 Copyright: © 2016 Sonu Mishra et.al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
منابع مشابه
Antigenic determinants in proteins coincide with surface regions accessible to large probes (antibody domains).
We evaluated surface areas on proteins that would be accessible to contacts with large (1-nm radius) spherical probes. Such spheres are comparable in size to antibody domains that contain antigen-combining sites. We found that all the reported antigenic sites correspond to segments particularly accessible to a large sphere. The antigenic sites were also evident as the most prominently exposed r...
متن کاملRelationship of cell surface hydrophobicity with biofilm formation and growth rate: A study on Pseudomonas aeruginosa, Staphylococcus aureus, and Escherichia coli
Objective(s): This study was designed to determine the relationship of Pseudomonas aeruginosa, Staphylococcus aureus, and Escherichia coli isolates in multispecies biofilms and their individual phenotypic characters in biofilm consortia. Materials and Methods: The subject isolates were recovered from different food samples and identified on the basis of growth on differential and selective med...
متن کاملProtein Electrostatic Properties Predefining the Level of Surface Hydrophobicity Change upon Phosphorylation
We use explicit-solvent, molecular dynamics simulations to study the change in polar properties of a solvent-accessible surface for proteins undergoing phosphorylation. We analyze eight different pairs of proteins representing different structural classes in native and phosphorylated states and estimate the polarity of their surface using the molecular hydrophobicity potential approach. Whereas...
متن کاملMethaemoglobin Content and NADH-Methaemoglobin Reductase Activity of Three Human Erythrocyte Genotypes
Background: To study methaemoglobin content and NADH-methaemoglobin reductase activity of three human erythrocyte genotypes (HbAA, HbAS and HbSS).Materials and Methods: Studies to ascertain methaemoglobin concentration and level of NADH-methaemoglobin reductase activity of three human erythrocyte genotypes (HbAA, HbAS and HbSS) were carried out in forty-three (43) healthy male participants of c...
متن کاملThe Lipophilicity Examination of Some ACE inhibitors and Hydrochlorothiazide on Cellulose in RP Thin-Layer Chromatography
In this assay, the evaluation of lipophilicity of four ACE-inhibitors and hydrochlorothiazide (HCTZ) with RP-TLC on cellulose layers was described using three binary solvent systems. The selected ACE inhibitors had sufficiently different structures which can indicate the method suitability for their lipophilicity evaluation as the model substances in comparison with HCTZ. In addition, the linea...
متن کامل