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Thin layers of synthetic homopolypeptides (poly-α-Ala, -Arg, -Asn, -Asp, -Glu, -His, -Lys and -Tyr) and proteins (myoglobin, concanavalin A, trypsin-inhibitor) were irradiated under solid state conditions in an electron microscope with 100 keV electrons. Radiolytic changes were investigated by amino acid analysis. The results are discussed in terms of the relative radiosensitivities of the constituent amino acids, and possible topochemical effects on the sensitivity pattern emerging. An attempt is also made to trace at least some of the predominant pathways of amino acid transformation, namely the production of alanine and a-aminobutyric acid

Radiation Damage to Polypeptides and Proteins in the Solid State: Changes in Amino Acid Composition *