Denaturation of the tryptic fragments of the calcium (II) adenosine triphosphatase from sarcoplasmic reticulum by guanidinium hydrochloride.
Primary and secondary fragments of the Ca2+-adenosine triphosphatase from sarcoplasmic reticulum are resistant to complete denaturation by guanidinium hydrochloride, a property characteristic of many intrinsic membrane proteins. None of the fragments display a single cooperative transition from ordered structure to random coil suggesting each fragment contains several domains of differing resistance to guanidinium hydrochloride denaturation. The data suggest that the native enzyme has at least three membrane-embedded domains, with an externally accessible link between each.
D000478:Alkylation; D000818:Animals; D000252:Calcium-Transporting ATPases; D002942:Circular Dichroism; D006146:Guanidines; D007700:Kinetics; D010084:Oxidation-Reduction; D010446:Peptide Fragments; D011487:Protein Conformation; D011489:Protein Denaturation; D012519:Sarcoplasmic Reticulum / Q000201:enzymology*; D014357:Trypsin
D006146:Guanidines; D010446:Peptide Fragments; D014357:Trypsin; D000252:Calcium-Transporting ATPases