Rosette Nanotube Porins as Ion Selective Transporters and Single-Molecule Sensors | Journal of the American Chemical Society
Prokaryotic and Eukaryotic Porins: Comparison of Structure and Function | SpringerLink
Topology of the Porin MspA in the Outer Membrane of Mycobacterium smegmatis - ScienceDirect
Gram-negative trimeric porins have specific LPS binding sites that are essential for porin biogenesis | PNAS
Mary bellamy hi-res stock photography and images - Alamy
MCQ FOR PLANT PATHOLOGY ASRB NET / PREVIOUS PAPER PLANT PATHOLOGY/ MCQ FOR ICAR NET PLANT PATHOLOGY - YouTube
Vaxxon SRP Salmonella-50 Dose
Analytical Approaches for Studying Transporters, Channels and Porins | Chemical Reviews
Design, assembly, and characterization of membrane-spanning DNA nanopores | Nature Protocols
Analytical Approaches for Studying Transporters, Channels and Porins | Chemical Reviews
Rosette Nanotube Porins as Ion Selective Transporters and Single-Molecule Sensors | Journal of the American Chemical Society
Prokaryotic and Eukaryotic Porins: Comparison of Structure and Function | SpringerLink
Gram-negative trimeric porins have specific LPS binding sites that are essential for porin biogenesis | PNAS
Prokaryotic and Eukaryotic Porins: Comparison of Structure and Function | SpringerLink
Prokaryotic and Eukaryotic Porins: Comparison of Structure and Function | SpringerLink
Membrane Proteins & its types | PPT
Gram-negative trimeric porins have specific LPS binding sites that are essential for porin biogenesis | PNAS
Prokaryotic and Eukaryotic Porins: Comparison of Structure and Function | SpringerLink
Folding and Misfolding of Human Membrane Proteins in Health and Disease: From Single Molecules to Cellular Proteostasis | Chemical Reviews
Building membrane nanopores | Nature Nanotechnology
Robins & Morton (@RobinsMorton) / X
Gram-negative trimeric porins have specific LPS binding sites that are essential for porin biogenesis | PNAS
Prokaryotic and Eukaryotic Porins: Comparison of Structure and Function | SpringerLink
Sandbox porins - Proteopedia, life in 3D
Crystal structure of Omp32, the anion-selective porin from Comamonas acidovorans, in complex with a periplasmic peptide at 2.1 Å resolution - ScienceDirect
