New type of representation for mapping chain-folding in protein molecules

Abstract

CONFORMATIONAL details of small molecules can easily be visualised in the usual stereo diagrams used by crystallographers, but such details cannot be readily visualised for protein molecules made up of thousands of atoms. For such large molecules special types of representations become necessary for depicting their three-dimensional structure, in the form of two-dimensional diagrams. In view of this, many attempts to represent the conformational details in protein molecules, have been reported^1–7. I present here a new method for mapping the folding of the backbone polypeptide chain of protein molecules. This representation brings out all the features of protein folding, with no degeneracy caused by depicting the conformational details, and is useful in readily recognising all the secondary structures, without ambiguity, as one progresses along the chain.