HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Bianchi, E. Articles by Rajagh, L. Search for Related Content PubMed PubMed Citation Articles by Bianchi, E. Articles by Rajagh, L. Social Bookmarking                      What's this?

The Role of pH, Temperature, Salt Type, and Salt Concentration on the Stability of the Crystalline, Helical, and Randomly Coiled Forms of Collagen

From the ¹ From the Istituto di Chimica Industriale dell' Universita', Genova, Italy
² From the Chemstrand Research Center, Inc., Durham, North Carolina 27702

The role of pH, temperature, salt type, and salt concentration on the three possible transformations involving the crystalline, dispersed helical, and randomly coiled forms of collagen has been investigated. The results are given in terms of pseudo phase diagrams where the field of stability of each form is delimited by the curves representing the variation of the three transformation temperatures with salt concentration for a given salt type and pH. The data are adequate to characterize the behavior of the systems corresponding to situations where the solute is an isoelectric protein or a cationic polyelectrolyte.

It is shown that a general mechanism for the interaction between salts and proteins based on the previously defined specific (i.e. binding) and diluent effects, is adequate to describe the transformations crystalline form randomly coiled form, crystalline form helical form, helical form randomly coiled form under isoelectric conditions. The polyelectrolyte behavior included the reversal of the orders of effectiveness of anions with respect to the orders observed under isoelectric conditions. This is explained on the basis of an order for binding of the anions to the solute which remains the same irrespective of whether the protein is iso-electric or cationic.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				U. Freudenberg, S. H. Behrens, P. B. Welzel, M. Muller, M. Grimmer, K. Salchert, T. Taeger, K. Schmidt, W. Pompe, and C. Werner Electrostatic Interactions Modulate the Conformation of Collagen I Biophys. J., March 15, 2007; 92(6): 2108 - 2119. [Abstract] [Full Text] [PDF]

				K. Kar, P. Amin, M. A. Bryan, A. V. Persikov, A. Mohs, Y.-H. Wang, and B. Brodsky Self-association of Collagen Triple Helic Peptides into Higher Order Structures J. Biol. Chem., November 3, 2006; 281(44): 33283 - 33290. [Abstract] [Full Text] [PDF]