Hydrophobic Mapping of Chlorobium Tepidum, the Energy Generating Bacteria

Chowdhury, Anindita Roy; Kothari, Anushka

doi:10.30876/johr.7.3.2019.98-106

Cited by 1 publication

(3 citation statements)

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“…As the statistical distribution of hydrophobic residues was involved in this investigation, an experimental method-based scale known as Fauchere-Pliska hydrophobicity scale was preferred [25,28]. In many biophysical, bioinformatics, and pharmacological investigations, this scale is effective [27,[29][30][31][32][33].…”

Section: Hydrophobic Scalementioning

confidence: 99%

“…C + + program was executed on the downloaded fasta sequences of the spike proteins of SARS-CoV-2 and SARS-CoV as well as their aligned sequences to determine the hydrophobic strength [29][30][31]. The output files of the program showed the specific hydrophobic details for each protein sequence of the spike proteins of SARS-CoV-2 and SARS-CoV.…”

Section: Calculation Of Hydrophobic Contributionmentioning

confidence: 99%

“…Hydrophobic contribution was calculated on the basis of the frequency of occurrence of respective amino acids in a protein sequence and their hydrophobic scale value [29][30][31]. The total hydrophobic contribution of all aromatic residues was considered and mentioned as TAroH (i.e., WH, FH, YH, and HH); TAliH (IH, LH, CH, VH, PH, AH, and MH) stated the same for all aliphatic residues.…”

Section: Calculation Of Hydrophobic Contributionmentioning

confidence: 99%

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Computational and comparative investigation of hydrophobic profile of spike protein of SARS-CoV-2 and SARS-CoV

Shekhawat

Chowdhury

2022

J Biol Phys

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The hydrophobic force is one of the most dominant factors in protein folding. A protein becomes functional only when it achieves its three-dimensional structure and stability upon folding. For a better understanding of the hydrophobic effects and their function in protein folding, quantitative measurement of the hydrophobicity of amino acid side chains is crucial. Spike protein is the primary structural protein in SARS-CoV-2 and SARS-CoV. This study explores how protein sequences in SARS-CoV-2 and SARS-CoV spike proteins encode hydrophobic interactions. Computational tools/techniques have been utilized to investigate the protein sequences of the spike proteins of SARS-CoV-2 and SARS-CoV. Investigations provided an estimate of hydrophobic distribution and its relative strength, indicating a hydrophobic pattern. Analysis of the spike protein's hydrophobic profile may help identify and treat the virus-caused disease; additionally, it can give an insight into the transmissibility and pathogenicity of the virus. Supplementary Information The online version contains supplementary material available at 10.1007/s10867-022-09615-x.

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