accessible surfaces of beta proteins increase with increasing protein molecular mass more rapidly than those of other proteins访问表面β蛋白的增加与增加蛋白质分子质量比其他蛋白质更迅速.pdfVIP

Accessible Surfaces of Beta Proteins Increase with Increasing Protein Molecular Mass More Rapidly than Those of Other Proteins 1,2 1 1 Anna V. Glyakina , Natalya S. Bogatyreva , Oxana V. Galzitskaya * 1 Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, Russia, 2 Institute of Mathematical Problems of Biology, Russian Academy of Sciences, Pushchino, Moscow Region, Russia Abstract Here we present a systematic analysis of accessible surface areas and hydrogen bonds of 2554 globular proteins from four structural classes (all-a, all-b, a/ b and a+b proteins) that is aimed to learn in which structural class the accessible surface area increases with increasing protein molecular mass more rapidly than in other classes, and what structural peculiarities are responsible for this effect. The beta structural class of proteins was found to be the leader, with the following possible explanations of this fact. First, in beta structural proteins, the fraction of residues not included in the regular secondary structure is the largest, and second, the accessible surface area of packaged elements of the beta-structure increases more rapidly with increasing molecular mass in comparison with the alpha-structure. Moreover, in the beta structure, the probability of formation of backbone hydrogen bonds is higher than that in the alpha helix for all residues of a+b proteins (the average probability is 0.7360.01 for the beta-structure and 0.60 60.01 for the alpha-structure without proline) and a/ b proteins, except for asparagine, aspartic acid, glycine, threonine, and serine (0.7060.01 for the beta-structure and 0.60 60.01 for the alpha-structure without the proline residue). There is a linear relationship between