Variable denaturation of ovalbumin by incorporation of amino acid analogs.
Denaturation of hen ovalbumin synthesized in a cell-free system was assayed by examining its sensitivity to trypsin. The native ovalbumin resisted digestion by trypsin, and it remained resistant to digestion when some amino acid analogs, including azetidine-2-carboxylic acid and meta-flourotyrosine, were incorporated into its peptide chain. However, when other amino acid analogs such as beta-hydroxyleucine and 4-thiaisoleucine were incorporated during protein systhesis, ovalbumin became very lablie to trypsin. These experiments demonstrate a sensitive system for detecting protein denaturation and suggest a variable effect of different amino acid analogs on the native conformation of a protein.
D000818:Animals; D002287:Carcinoma, Krebs 2 / Q000378:metabolism; D002474:Cell-Free System; D002645:Chickens; D005260:Female; D051379:Mice; D010047:Ovalbumin / Q000235:genetics*; D011489:Protein Denaturation; D012333:RNA, Messenger / Q000235:genetics; D012270:Ribosomes / Q000378:metabolism; D014357:Trypsin / Q000378:metabolism
D012333:RNA, Messenger; D010047:Ovalbumin; D014357:Trypsin