Modelling of structure and function of proteins and nucleic acids.

The native conformation of a linear biopolymer is, under physiological conditions, exclusively determined by the sequence of the side chains. The task of predicting the native structure on the sequence basis remains unsolved. In this paper we present our attempts to describe and predict conformations of biopolymers undertaken at the Institute of Biochemistry and Biophysics, Polish Academy of Sciences in Warsaw in collaboration with groups of W.

The formation of protein secondary structure. Its connection with amino acid sequence.

Statistical analysis of the occurrence of tetrapeptides in 35 globular proteins was performed. It was found that the amino acids along the polypeptide chain are close to being randomly distributed and that the same tetrapeptide segments exist in different types of secondary structure. Therefore, a new method was proposed for locating 'microdomains' in protein interiors.

Hydrophobic microdomains as structural invariant regions in proteins.

A procedure for finding clusters of interacting residues in protein hydrophobic cores is proposed. Such clusters have been located for six globular proteins of known structure. Assuming that sequences of the same protein from different biological sources encode the same tertiary structure, replacements within clusters were analysed after sequence alignment.

Methods of molecular modelling of protein-protein interactions.

This article reviews briefly theoretical methods attempting to predict the structure of protein aggregates from the structural features of their subunits. The authors discuss the problems of the solvent effect and the formation of protein structure. The existing methods of quaternary structure prediction are presented and an attempt at their classification is made at the end of this review.

Prediction of the beta Bp crystallin dimer structure by the complementary surfaces (CS) method.

The method of searching for complementary surfaces of proteins was used to evaluate the modes of beta Bp crystallin autoassociation. The dimer structure of beta Bp is predicted and characterized.