Moments of the distributions of the Cα and side-chain atoms and assocd. properties were examd. in 22 globular proteins, considered as statistical aggregates of atoms. Although the distributions are generally anisotropic, the densities of the evaluated distributions are highly uniform in the interior of a single protein, as well as among the proteins investigated. The tertiary structure of proteins is characterized by a compact and uniform distribution of amino acids, independent of their mol. wt. and hydrophobic character, and by an isotropic distribution of the virtual bond directions in the polypeptide folding. Whereas the general uniformity of the d. of distributions in the bulk of proteins can be justified by the architectural requirements of high thermodn. stability, significant differences in the distribution of the Cα with respect to the side-chain atoms suggest a plausible explanation of the general anisotropic morphol. of the proteins. The invariance of the d. of distributions allows easy recognition of proteinlike domains in more complex proteins and suggests a practical way to predict the following path in single proteins.

Moments of the distribution of the amino acid residues in tertiary structures of globular proteins / DE SANTIS, Pasquale; Morosetti, Stefano; Palleschi, Antonio. - In: BIOPOLYMERS. - ISSN 0006-3525. - STAMPA. - 18:12(1979), pp. 2963-2978. [10.1002/bip.1979.360181205]

Moments of the distribution of the amino acid residues in tertiary structures of globular proteins

DE SANTIS, Pasquale;MOROSETTI, Stefano;PALLESCHI, Antonio
1979

Abstract

Moments of the distributions of the Cα and side-chain atoms and assocd. properties were examd. in 22 globular proteins, considered as statistical aggregates of atoms. Although the distributions are generally anisotropic, the densities of the evaluated distributions are highly uniform in the interior of a single protein, as well as among the proteins investigated. The tertiary structure of proteins is characterized by a compact and uniform distribution of amino acids, independent of their mol. wt. and hydrophobic character, and by an isotropic distribution of the virtual bond directions in the polypeptide folding. Whereas the general uniformity of the d. of distributions in the bulk of proteins can be justified by the architectural requirements of high thermodn. stability, significant differences in the distribution of the Cα with respect to the side-chain atoms suggest a plausible explanation of the general anisotropic morphol. of the proteins. The invariance of the d. of distributions allows easy recognition of proteinlike domains in more complex proteins and suggests a practical way to predict the following path in single proteins.
1979
globular proteins statistics; hydrophobic amino acids distribution; moments of the distributions; structural domains
01 Pubblicazione su rivista::01a Articolo in rivista
Moments of the distribution of the amino acid residues in tertiary structures of globular proteins / DE SANTIS, Pasquale; Morosetti, Stefano; Palleschi, Antonio. - In: BIOPOLYMERS. - ISSN 0006-3525. - STAMPA. - 18:12(1979), pp. 2963-2978. [10.1002/bip.1979.360181205]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/382526
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