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pro vyhledávání: '"Ian S. Millet"'
Autor:
Judith Frydman, Anne S. Meyer, Dirk Walther, Joel R. Gillespie, Ian S. Millet, Sebastian Doniach
Publikováno v:
Cell. 113(3):369-381
Chaperonins use ATPase cycling to promote conformational changes leading to protein folding. The prokaryotic chaperonin GroEL requires a cofactor, GroES, which serves as a “lid” enclosing substrates in the central cavity and confers an asymmetry
Publikováno v:
Biochemistry. 41(1)
An important element of protein folding theory has been the identification of equilibrium parameters that might uniquely distinguish rapidly folding polypeptide sequences from those that fold slowly. One such parameter, termed sigma, is a dimensionle