Conformation of glycyl residues in globular proteins

Abstract

Glycine is unique among the amino acids in view of its symmetric nature. While the overall distribution of glycyl residues in the (.vphi., .psi.) plane is near-symmetric, there can be certain preferences for the individual conformations. An analysis of the observed glycyl conformations in 70 proteins has been carried out to find the influence of residues adjoining the glycyl residues. For this purpose, the (.vphi., .psi.) plane has been divided into two regions: (a) the region in which .vphi. is negative and (b) the region in which .vphi. is positive. The analysis is done in terms of the number of conformations occurring in these regions. It has been found that while the overall percentage distribution of glycyl residues between the positive and the negative .vphi. regions is 54:46, the distribution shows asymmetry when the examples are sorted out in terms of X-Gly and Gly-Y doublets. The asymmetry becomes more prominent when the data are sorted out into triplets X-Gly-Y. Using the available information, it has been possible to designate 25 triplets as P-predominant and 19 as N-predominant. An examination of P-predominant triplets for possible occurrence in .beta.-bends having one of the conformations in the positive .vphi. region shows that only 25% are of this nature. Thus, the P-preference of P-predominant triplets is not an outcome of the bend formation alone and must be an inherent property of these triplets.