Temperature Effects on Free Radical Formation and Electron Migration in Irradiated Proteins

Journal Article · Mon Aug 01 04:00:00 EDT 1960 · Proceedings of the National Academy of Sciences of the United States of America

DOI:https://doi.org/10.1073/pnas.46.8.1137· OSTI ID:4167536

Patten, F.; Gordy, W.

Electron vacancy, or electron spin density, caused by irradiation was found, at room temperature, to migrate through the protein from the multiple sites where the ionizing radiation struck to the few sites where the spin density was finally detected. Such migration did not occur at the temperature of liquid nitrogen, 77 deg K. From the shape of their resonances, it was concluded that when silk and feather quill were irradiated at temperatures as low as 77 deg K, several types of free radicals were produced. When the proteins irradiated at lowered temperatures were allowed to warm to room temperature, these complex patterns were usually converted to the simple pattern of a single free radical. This radical was the one characteristic of that protein irradiation at room temperature. A possible mechanism for this formation of characteristic free radicals is described. (M.C.G.)

• Research Organization: Duke Univ., Durham, N.C.
• Sponsoring Organization: USDOE
• NSA Number: NSA-14-022733
• OSTI ID: 4167536
• Journal Information: Proceedings of the National Academy of Sciences of the United States of America, Journal Name: Proceedings of the National Academy of Sciences of the United States of America Journal Issue: 8 Vol. 46; ISSN 0027-8424
• Publisher: National Academy of Sciences, Washington, DC (United States)
• Country of Publication: Country unknown/Code not available
• Language: English

Related Subjects

BIOCHEMISTRY
BIOLOGY AND MEDICINE
CELLULOSE
ELECTRONS
FEATHERS
FREE RADICALS
IRRADIATION
LOW TEMPERATURE
PROTEINS
QUALITATIVE ANALYSIS
RADIATION EFFECTS
RESONANCE
SILK
SKIN
SPIN
TEMPERATURE
VARIATIONS