Natalia Lisitza1, Xudong Huang2, Hiroto Hatatu3, Samuel Patz3
1Department of Radiology, Brigham & Women's Hospital, Harvard Medical School, Boston, MA, United States; 2Department of Psychiatry, Massachusetts General Hospital, Harvard Medical School, Boston, MA, United States; 3Department of Radiology, Brigham & Womens Hospital, Harvard Medical School, Boston, MA, United States
In this study we use NMR to explore collagen self-aggregation. We observe an abrupt change of the total collagen NMR signal intensity at a critical concentration where self-aggregation starts. We measure the NMR spectrum of collagen as function of protein concentration and detect changes of this dependence in time; we relate these changes to collagen aggregation. We show that the concentration dependence of the collagen NMR signal is sensitive to pH and that this behavior correlates with aggregation mechanisms proposed in literature. The advantage of NMR is that it allows noninvasive investigation of biological systems in solution, preserving their physiological conformations and functions.