Disulfide bonding in protein biophysics.
It has been known for many decades that cell surface, soluble-secreted, and extracellular matrix proteins are generally rich in disulfide bonds, but only more recently has the functional diversity of disulfide bonding in extracellular proteins been appreciated. In addition to the classic mechanisms by which disulfide bonds enhance protein thermodynamic stability, disulfides in certain configurations contribute particular mechanical properties to proteins that sense and respond to tensile forces. Disulfides may help warp protein folds for the evolution of new functions, or they may fasten aggregation-prone flaps of polypeptide to protein surfaces to prevent fibrilization or oligomerization. Disulfides can also be used to package and secure macromolecular cargo for intercellular transport. A series of case studies illustrating diverse biophysical roles of disulfide bonding are reviewed, with a focus on proteins functioning in the extracellular environment.
Department of Structural Biology, Weizmann Institute of Science, Rehovot 76100, Israel. deborah.fass@weizmann.ac.il
Deborah
D
Fass
D000818:Animals; D001696:Biomechanical Phenomena; D003545:Cysteine / Q000737:chemistry / Q000378:metabolism; D004220:Disulfides / Q000737:chemistry / Q000378:metabolism; D055550:Protein Stability; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D013816:Thermodynamics
D004220:Disulfides; D011506:Proteins; D003545:Cysteine