Beta-II conformation of all-beta proteins can be distinguished from unordered form by circular dichroism.
The CD spectrum of certain all-beta globular proteins resembles that of unfolded proteins with a characteristic negative band around 200 nm. The conformation of this class is tentatively termed beta-II, which had two features that were absent for unfolded proteins. First, beta-II proteins usually had CD bands due to aromatic side groups in the near-ultraviolet region. Second, the CD intensities both in the far- and in the near-uv region of these compact and rigid proteins usually showed a sharp transition upon thermal denaturation, whereas those of an unordered form changed linearly with rising temperature.
Wu
J
J
Cardiovascular Research Institute, University of California, San Francisco 94143-0524.
Yang
J T
JT
Wu
C S
CS
D002918:Chymotrypsin / Q000737:chemistry; D002942:Circular Dichroism; D010196:Pancreatic Elastase / Q000737:chemistry; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D013056:Spectrophotometry, Ultraviolet / Q000379:methods; D013816:Thermodynamics; D014361:Trypsin Inhibitors / Q000737:chemistry
D011506:Proteins; D014361:Trypsin Inhibitors; D002918:Chymotrypsin; D010196:Pancreatic Elastase