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pro vyhledávání: '"S G, Burston"'
Publikováno v:
Journal of molecular biology. 293(3)
Single-point mutants of GroEL were constructed with tryptophan replacing a tyrosine residue in order to examine nucleotide-induced structural transitions spectrofluorometrically. The tyrosine residues at positions 203, 360, 476 and 485 were mutated.
Publikováno v:
Methods in enzymology. 290
Autor:
S G, Burston, A R, Clarke
Publikováno v:
Essays in biochemistry. 29
Molecular chaperones can be broadly defined as proteins which interact with non-native states of other protein molecules. This activity is important in the folding of newly synthesized polypeptides and the assembly of multisubunit structures; the mai