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Structural Stability Analysis of Proteins Using End-to-End Distance: A 3D-RISM Approach.
- Source :
- J: Multidisciplinary Scientific Journal; Mar2022, Vol. 5 Issue 1, p114-125, 12p
- Publication Year :
- 2022
-
Abstract
- The stability of a protein is determined from its properties and surrounding solvent. In our previous study, the total energy as a sum of the conformational and solvation free energies was demonstrated to be an appropriate energy function for evaluating the stability of a protein in a protein folding system. We plotted the various energies against the root mean square deviation, required as a reference structure. Herein, we replotted the various energies against the end-to-end distance between the N- and C-termini, which is not a required reference and is experimentally measurable. The solvation free energies for all proteins tend to be low as the end-to-end distance increases, whereas the conformational energies tend to be low as the end-to-end distance decreases. The end-to-end distance is one of interesting measures to study the behavior of proteins. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 25718800
- Volume :
- 5
- Issue :
- 1
- Database :
- Complementary Index
- Journal :
- J: Multidisciplinary Scientific Journal
- Publication Type :
- Academic Journal
- Accession number :
- 156019503
- Full Text :
- https://doi.org/10.3390/j5010009