Structural characteristics of 1399 globular protein domains from classes α/β and α+β.

<p>Structural characteristics of 1399 globular protein domains from classes α/β and α+β.</p

Log-log dependences of accessible surface areas on protein molecular masses for four structural classes of proteins.

<p>Cases (A) and (C) for general dataset of proteins and cases (B) and (D) for re-refined protein structures. In cases (A) and (B), values for all proteins without averaging (the number of points corresponds to the number of proteins in each structural class) were considered. And in cases (C) and (D) these values were averaged in the given region of the protein lengths (six points for each structural class).</p

Average frequency of occurrence of each type of amino acid residue in four structural classes of proteins.

<p>Average frequency of occurrence of each type of amino acid residue in four structural classes of proteins.</p

Distribution of hydrogen bonds per residue in the given region of amino acid residues in four structural classes of proteins calculated with YASARA. Cases (A, C, E) without and (B, D, F) with energy minimization.

<p>Distribution of hydrogen bonds per residue in the given region of amino acid residues in four structural classes of proteins calculated with YASARA. Cases (A, C, E) without and (B, D, F) with energy minimization.</p

Structural characteristics of 1155 globular protein domains from classes α and β.

<p>Structural characteristics of 1155 globular protein domains from classes α and β.</p

Dependences of a number of hydrogen bonds on the number of amino acid residues in protein.

<p>Dependences of a number of hydrogen bonds on the number of amino acid residues in protein.</p

Log-log dependences of accessible surface areas on protein molecular masses for four structural classes of proteins where the fraction of loop residues in the protein structure is as follows: (A, C) 0.4–0.5; (B, D) 0.5–0.6.

<p>In cases (A) and (B), values for all proteins without averaging were considered (the number of points corresponds to the number of proteins in each structural class). And in cases (C) and (D) these values were averaged in the given region of protein lengths (six points for each structural class).</p

Average number of hydrogen bonds per residue for proteins with different resolutions.

<p>(A) Difference in the number of hydrogen bonds per residue after and before energy minimization (YASARA). (B) Number of hydrogen bonds per residue (DSSP).</p

Fraction of amino acid residues of each type of secondary structure.

<p>H, helix (α and 3₁₀); E, β structure; C, coil for four structural classes of proteins calculated using the DSSP (A) and YASARA (B) programs.</p

Log-log dependences of accessible surface areas on protein molecular masses for four structural classes of proteins where the number of loop residues per regular secondary structure element varies from 5 to 10.

<p>In case (A), values for all proteins without averaging were considered (the number of points corresponds to the number of proteins in each structural class). And in case (B) these values were averaged in the given region of protein lengths (six points for each structural class).</p