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Nanopore Analysis of a Small 86‐Residue Protein
Author(s) -
Stefureac Radu,
Waldner Landon,
Howard Peter,
Lee Jeremy S.
Publication year - 2008
Publication title -
small
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.785
H-Index - 236
eISSN - 1613-6829
pISSN - 1613-6810
DOI - 10.1002/smll.200700402
Subject(s) - nanopore , mutant , residue (chemistry) , biophysics , chemistry , chromosomal translocation , cytoplasm , amino acid , mutation , nanotechnology , crystallography , biochemistry , materials science , biology , gene
HPr is a small protein that must unfold to translocate the α‐hemolysin pore (see image). Single amino acid substitutions can cause large changes to the translocation parameters. A conservative mutation is sufficient to alter the event profile; either the mutant must unfold differently or it must interact with the pore differently. A negatively charged mutant is driven through the pore, which facilitates unfolding.