Time differential perturbed angular correlation of 111In-EDTA linked to the single free cysteine of bovine serum albumin.
By means of a facile chemical modification of the bovine serum albumin molecule, it was possible to measure its hydrodynamic radius with high accuracy (approximately 3%) using the TDPAC technique. The new approach presented here allows a wide use of the TDPAC technique to perform high precision studies of backbone dynamics of almost any protein.
Ceolín
M
M
Departamento de Física, Facultad de Ciencias Exactas, Universidad Nacional de La Plata, Argentina. marcelo@venus.fisica.unlp.edu.ar
Martínez
J A
JA
Ermácora
M R
MR
D000818:Animals; D002417:Cattle; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003545:Cysteine / Q000737:chemistry* / Q000378:metabolism; D004492:Edetic Acid / Q000737:chemistry* / Q000378:metabolism; D007205:Indium Radioisotopes; D008968:Molecular Conformation; D012710:Serum Albumin, Bovine / Q000737:chemistry* / Q000378:metabolism; D013057:Spectrum Analysis / Q000379:methods; D013997:Time Factors
D007205:Indium Radioisotopes; D012710:Serum Albumin, Bovine; D004492:Edetic Acid; D003545:Cysteine