NalP: Difference between revisions
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The Translocator Domain for the Autotransporter NaIP within Neisseria meningitidis provides a novel protein pore that contains an alpha helix running axially through its hydrophilic center. Classically many outer membrane pores contain a 12-member beta barrel, which is able to allow for different conditions than the peptidoglycan layer that would typically stop many types of proteins and ions from passing through. This alpha helix blocks the pore from being totally open and allows for more regulation of what enters and leaves the cell. | The Translocator Domain for the Autotransporter NaIP within Neisseria meningitidis provides a novel protein pore that contains an alpha helix running axially through its hydrophilic center. Classically many outer membrane pores contain a 12-member beta barrel, which is able to allow for different conditions than the peptidoglycan layer that would typically stop many types of proteins and ions from passing through. This alpha helix blocks the pore from being totally open and allows for more regulation of what enters and leaves the cell. | ||
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