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Counterpoint: Statistical analysis in NIH peer review--identifying innovation.
Defining the structure of the substrate-free state of the DnaK molecular chaperone.
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Defining the structure of the substrate-free state of the DnaK molecular chaperone.
Swain JF, Sivendran R, Gierasch LM. Defining the structure of the substrate-free state of the DnaK molecular chaperone. Biochem Soc Symp. 2001; (68):69-82.
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subject areas
Binding Sites
Escherichia coli
Escherichia coli Proteins
HSP70 Heat-Shock Proteins
Hydrogen-Ion Concentration
Magnetic Resonance Spectroscopy
Models, Molecular
Molecular Chaperones
Mutagenesis, Site-Directed
Peptide Fragments
Protein Conformation
Protein Folding
Spectrometry, Fluorescence
Tryptophan
authors with profiles
Lila M Gierasch Ph.D.