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pro vyhledávání: '"Luke D. Heskett"'
Publikováno v:
Protein Science. 12:1205-1215
The GrpE heat shock protein from Escherichia coli has a homodimeric structure. The dimer interface encompasses two long alpha-helices at the NH(2)-terminal end from each monomer (forming a "tail"), which lead into a small four-helix bundle from which
Publikováno v:
Biochemical and biophysical research communications. 282(2)
A key feature to the dimeric structure for the GrpE heat shock protein is the pair of long helices at the NH,-terminal end followed by a presumable extended segment of about 30 amino acids from each monomer. We have constructed a GrpE deletion mutant