Recognition of a transmembrane domain: another role for the ribosome?

Article Abstract:

The translocation of process of proteins from the membrane of the endoplasmic reticulum (ER) during protein synthesis was dependent on the presence of ribosomes. Ribosomes acted as critical cofactors that mediated the recognition of signal sequences on ER-directed proteins by the signal recognition particles. On the other hand, the signal recognition particles acted as cytoplasmic ribonucleoproteins that promote protein targeting in the ER.

Endoplasmic reticulum, Carrier proteins, Transport proteins, Biological transport, Active, Active biological transport

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Backbone mutations in transmembrane domains of a ligand-gated ion channel: implications for the mechanism of gating

Article Abstract:

A study was conducted to analyze a way to determine backbone conformational changes associated with nicotinic acetylcholine receptor gating. The model supports changes of backbone conformation within the M2 domain. In addition, nAChR channels are characterized by wild-type function and differences associated with standard mutagenesis. Results showed that a conserved proline in the M1 domain supports a critical function in nAChR gating.

Ion channels, Ligands, Ligands (Chemistry)

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