Volume 17, Issue 65 (4-2008)                   JGUMS 2008, 17(65): 117-127 | Back to browse issues page

XML Persian Abstract Print


Download citation:
BibTeX | RIS | EndNote | Medlars | ProCite | Reference Manager | RefWorks
Send citation to:

Forouhi E. A Hydrophobicity Scale for the Amino Acids. JGUMS 2008; 17 (65) :117-127
URL: http://journal.gums.ac.ir/article-1-335-en.html
Abstract:   (6253 Views)
Abstract Introduction: The hydrophobic interaction is a major driving force behind many effects and phenomena in biological systems many hydrophobicity scales have already been proposed and have been used to predict the topography of proteins. Objective: In the present work based on some theoretical considerations a new hydrophobic scale for the amino acids is proposed. Materials and Methods: From the empirically justified assumptions that hydrophobicity of the amino acid residues as part of a polypeptide chain is dependent on the surface area and the electronegativity content of the residues, an equation which relates the hydrophobicity to the surface area and the number, and electro negativity of oxygen and nitrogen of the residue is proposed. From this equation a new hyrophobicity scale for the amino acids is obtained. Using this scale and a sliding window averaging method hrdrophobicity plots for the human melatonin receptor and prion protein (the cause of mad cow disease) are drawn and the intramembrane structure of melatonin mel1a receptor and hydrophobic core of the second half of the prion protein are determined and compared with those from literatures. Results: the proposed hydrophobicity scale in this work is in good agreement with that of Engelmann and coworkers. The intramembrane structure of melatonin receptor and the structure of the hydrophobic core of the prion protein predicted in this article are in good agreement with those proposed in the literatures. Conclusion: the proposed hydrophobicity scale in this work is suitable for predicting the topography of the tran membrane and globular proteins.
Full-Text [PDF 3531 kb]   (1684 Downloads)    
Review Paper: Research | Subject: Special
Received: 2013/12/22 | Accepted: 2013/12/22 | Published: 2013/12/22

Add your comments about this article : Your username or Email:
CAPTCHA

Rights and permissions
Creative Commons License This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License.

© 2024 CC BY-NC 4.0 | Journal of Guilan University of Medical Sciences

Designed & Developed by : Yektaweb