Multistep transitions in collagens

Abstract

It is well known that collagens exist in triple-helical form, and, on average, the individual chains have glycine at every third place. Collagens from different sources vary in distributions of other amino acids. They could also be different in the distribution of defects, which are generally nonhelical regions of low stability. Varying lengths of individual chains in the triple-helical system can also contribute to this variability. All these variations manifest themselves in the creation of a transition profile with undulations that are indicative of a multiphasic nature. In the present communication, we try to understand this variability by using essentially the Zimm and Bragg approach and suitably amending it for a triple-helical system. Factors that contribute to the multiphasic nature are incorporated into the transition model and discussed. Results obtained for collagen types I, II, III, Vx, Vy, and XI are in agreement with the experimental measurements. Transitions in the first three types can be interpreted on the basis of two-phase theory. Nucleation parameters, which are indicative of the sharpness of transition, are interpreted in terms of stability and possible amino acid composition.