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Banana Inflorescence and to Find the Interactions on Molecular Docking for PCOS
Published in Parimelazhagan Thangaraj, Phytomedicine, 2020
M. C. Kamaraj, Suman Thamburaj, R. Akshaya, V. Bhanu Deepthi
The human gene has the name CYP17A (P05093), the term polycystic ovarian syndrome was used as the protein, and it was retrieved from the SWISSPROT in the FASTA format. The primary physiochemical parameters were performed, and the amino acid composition was identified, and the details are given in Table 9.2. The results represented that the CYP17A protein is composed of 22 amino acids with different ratios. Among them, the leucine content was found to be more (12.6%), and that indicated the hydrophobic nature of the protein because it has an aliphatic isobutyl side chain and also essential amino acids. The molecular weight of the protein was found to be 57,370.52, and the protein has 8.72 isoelectric points that represent the protein is alkaline in nature. The extinction coefficient was 63,160 at 280 nm; it might be possible to avoid the interference of other substances. The evaluated value was used to determine the quantification of protein-protein or protein-ligand interactions. The quantitative measurement of the dynamic equilibrium was based on the half-life time. The CYP17A has 30 hours in mammalian reticulocytes, in yeast, it has 20, and 10 hours in E. coli, respectively. The stability of the protein was determined by using the instability index (33.18). The aliphatic index represented that the volume of the protein occupied by aliphatic chains (alanine, valine, isoleucine, and leucine), CYP17A, had a value of 99.80 that makes it more stable in high thermal conditions. Grand average hydropathicity denoted the hydrophobicity of the amino acid residues. Here, CYP17A with a value of −0.154 had a reasonable interaction with a water molecule. The protein molecule has four different atoms, such as C, H, N, O, and S, with the molecular formula of C2598H4116N698O731S17.
Investigating the effect of transcutol on the physical properties of an O/W cream
Published in Journal of Dispersion Science and Technology, 2020
Christopher Hernandez, Piyush Jain, Himanshu Sharma, Stephanie Lam, Sujatha Sonti
Emulsion stability against creaming was analyzed through the use of a LUMiSizer® Dispersion Analyzer. The LUMiSizer® uses STEP Technology to analyze a sample cell from top to bottom and has the ability to look at instability mechanisms such as creaming, sedimentation, flocculation, and coalescence. The instability index of a sample is defined as clarification achieved as a function of time divided by the maximum clarification possible. It is a dimensionless number, ranging between 0 and 1, which can be correlated with the level of phase separation due to creaming (0 = no separation, 1 = complete separation). Each formulation was tested at the most extreme conditions for the instrument (T = 40 °C and 4000 rpm) to force any potential separation and compare their stability under accelerated conditions. Figure 4 reveals that when the formulations were centrifuged at 40 °C, the creams became more unstable as the Transcutol® P concentrations were increased. The sharpest increase in the instability index was observed when the amount of Transcutol® P in the formulation was ≥25 (% w/w). The rate of separation can also be estimated using Stoke’s law. Using Stoke’s law, rate of separation in the formulation containing 40 (% w/w) Transcutol® P was found to occur three order of magnitudes faster than separation in the formulation containing 20 (% w/w) Transcutol® P. This shows that based on the density difference between the dispersed and continuous phases, the viscosity of the continuous phase, and approximate droplet size (estimated from microscopy images), the system containing a higher Transcutol® P content would separate faster. For the approximation here, Transcutol® P, propylene glycol, water, and Steareth-20 were assigned to the continuous phase, and medium chain triglycerides, Steareth-2, and CSA50 were assigned to the dispersed phase.
Identification and characterization of candidates involved in production of OMEGAs in microalgae: a gene mining and phylogenomic approach
Published in Preparative Biochemistry and Biotechnology, 2018
Vikas U. Kapase, Asha A. Nesamma, Pannaga P. Jutur
Various physico-chemical properties such as molecular weight, amino acid composition, stability, aliphatic index, and hydrophobicity were calculated using ExPASy’s ProtParam tool (Figure 3).[26,27] The molecular weight of OMEGA biosynthetic proteins ranges between 7183.22 and 171893.5 Da. It was observed that predicted pI values for all OMEGA proteins were basic in nature especially for 3-oxoacyl-[acyl-carrier-protein] reductase, stearoyl-CoA 9-desaturase, δ-12 desaturase, enoyl-CoA hydratase, acetyl-CoA acyltransferase, trans-2-enoyl-CoA reductase, acyl-CoA thioesterase, and 3-hydroxyacyl-CoA dehydratase; however, only acyl-CoA oxidase seems to be acidic in nature. The pI of the protein is significant in developing a buffer system during protein purification of the enzymes. Instability index helps us to distinguish between stable and unstable proteins by identifying the presence of certain dipeptides. The in vivo half-life of proteins can also co-related with instability index, indicating that the proteins with in vivo half-life >5 h have an instability index more than 40 and are assumed to be unstable whereas those with in vivo half-life >16 h have an instability index less than 40 and are predicted to be stable. The instability index of few proteins calculated was unstable and the reason may be due to inherent feedback mechanism that regulates the accumulation of cellular metabolites at optimal levels.[47] Our data show that δ-12 desaturase, acetyl-CoA acyltransferase, enoyl-CoA hydratase, and 3-oxoacyl-[acyl-carrier-protein] reductase are stable (Figure 3). The aliphatic index is directly related to the mole fraction of aliphatic side chains in the protein (alanine, isoleucine, leucine, and valine), and it will serve as a measure of thermostability in proteins. The aliphatic index of these proteins is within the range of 71.15–105.6. The presence of very high aliphatic index determines that their protein structures will be more stable at different ranges of temperatures.[40] The GRAVY index is the measure of solubility that indicates the nature of the protein. The increasing positive score indicates a greater hydrophobicity while negative score indicates hydrophilic in nature. In the present study, it was shown that 3-oxoacyl-[acyl-carrier-protein] reductase, 3-hydroxyacyl-CoA dehydratase, trans-2-enoyl-CoA reductase, and acetyl-CoA acyltransferase are hydrophobic, while others are hydrophilic in nature (Figure 3).