Effects of ultraviolet radiation on the type-I collagen protein triple helical structure: a method for measuring structural changes through optical activity.
A detailed study of the effects of ultraviolet radiation on type-I collagen has been conducted. We have confirmed that exposure to ultraviolet radiation lowers the denaturation temperature of type-I collagen and that the triple helical state is destroyed provided that the radiation dose exceeds a threshold level, which is defined as the incident radiation dose that raises the sample temperature above the (lower) denaturation temperature. For incident radiation doses below threshold, the collagen molecule remains in a triple helical state. Denaturation is determined by changes in the optical activity of the collagen solution. Furthermore, a new instrument has been developed and tested to measure the optical rotatory dispersion properties of chiral molecules. The advantage of this instrument is that it enables a real-time measurement of the optical activity of chiral macromolecules while exposing samples to ultraviolet radiation and requiring no special sample preparation techniques. Using a differential measurement scheme, system errors have been minimized.
Majewski
Alexander J
AJ
Physics and Engineering Physics Department, Stevens Institute of Technology, Hoboken, New Jersey 07030, USA.
Sanzari
Martin
M
Cui
Hong-Liang
HL
Torzilli
Peter
P
D000818:Animals; D002417:Cattle; D024042:Collagen Type I / Q000235:genetics*; D004247:DNA / Q000737:chemistry* / Q000528:radiation effects*; D004307:Dose-Response Relationship, Radiation; D055590:Electromagnetic Phenomena; D013696:Temperature; D014466:Ultraviolet Rays
D024042:Collagen Type I; D004247:DNA