Nanopore Analysis of a Small 86‐Residue Protein | Zendy

Stefureac Radu | Zendy; Waldner Landon | Zendy; Howard Peter | Zendy; Lee Jeremy S. | Zendy

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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.

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