Spatial and free energy distribution patterns of amino acid residues in water soluble proteins

We have calculated, for the 20 common amino acid residues: probability density functions that characterize the residues' tendency to occupy different locations in proteins; a propensity scale for the residues to be exposed or buried; mean force potentials that characterize the residues' fr...

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Veröffentlicht in:	Biophysical chemistry 1994-08, Vol.51 (2), p.327-336
Hauptverfasser:	Nauchitel, Vladimir V., Somorjai, Rajmund L.
Format:	Artikel
Sprache:	eng
Schlagworte:	Accessibility Amino Acid Sequence Amino Acids - chemistry Animals Chemical Phenomena Chemistry, Physical Hydrophobicity Models, Chemical Molecular Sequence Data Myoglobin - chemistry Plant Proteins - chemistry Proteins Proteins - chemistry Residues Solubility Thermodynamics Water - chemistry
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Zusammenfassung:	We have calculated, for the 20 common amino acid residues: probability density functions that characterize the residues' tendency to occupy different locations in proteins; a propensity scale for the residues to be exposed or buried; mean force potentials that characterize the residues' free energy dependence on their degree of exposure; the average composition of water soluble proteins, and the composition of their core and surface. The nature of differences between different hydrophobicity-related scales is discussed.
ISSN:	0301-4622 1873-4200
DOI:	10.1016/0301-4622(94)00053-0