[HTML][HTML] The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy
B Bechinger - Biochimica et Biophysica Acta (BBA)-Biomembranes, 1999 - Elsevier
Linear peptide antibiotics have been isolated from amphibians, insects and humans and
used as templates to design cheaper and more potent analogues for medical applications …
used as templates to design cheaper and more potent analogues for medical applications …
[HTML][HTML] Influenza M2 proton channels
M2 of the influenza virus is an intriguing transmembrane protein that forms a minuscule
proton channel in the viral envelope. Its recognized function is to equilibrate pH across the …
proton channel in the viral envelope. Its recognized function is to equilibrate pH across the …
[PDF][PDF] Imaging membrane protein helical wheels
Macromolecular structure determination by NMR spectroscopy has been absolutely
dependent on resonance assignments. Indeed, inaccurate assignments have frequently led …
dependent on resonance assignments. Indeed, inaccurate assignments have frequently led …
Histidines, heart of the hydrogen ion channel from influenza A virus: toward an understanding of conductance and proton selectivity
J Hu, R Fu, K Nishimura, L Zhang… - Proceedings of the …, 2006 - National Acad Sciences
The heart of the H+ conductance mechanism in the homotetrameric M2 H+ channel from
influenza A is a set of four histidine side chains. Here, we show that protonation of the third …
influenza A is a set of four histidine side chains. Here, we show that protonation of the third …
Structure and function of the influenza A M2 proton channel
The M2 protein of influenza A viruses forms a tetrameric pH-activated proton-selective
channel that is targeted by the amantadine class of antiviral drugs. Its ion channel function …
channel that is targeted by the amantadine class of antiviral drugs. Its ion channel function …
Protonation of histidine and histidine− tryptophan interaction in the activation of the M2 ion channel from influenza A virus
A Okada, T Miura, H Takeuchi - Biochemistry, 2001 - ACS Publications
The M2 protein of influenza A virus forms a homotetramer ion channel in the lipid
membrane. The channel is specific for proton conductance and is activated by low pH with a …
membrane. The channel is specific for proton conductance and is activated by low pH with a …
Structure and Mechanism of the Influenza A M218–60 Dimer of Dimers
We report a magic angle spinning (MAS) NMR structure of the drug-resistant S31N mutation
of M218–60 from Influenza A. The protein was dispersed in diphytanoyl-sn-glycero-3 …
of M218–60 from Influenza A. The protein was dispersed in diphytanoyl-sn-glycero-3 …
Functional studies indicate amantadine binds to the pore of the influenza A virus M2 proton-selective ion channel
X **g, C Ma, Y Ohigashi, FA Oliveira… - Proceedings of the …, 2008 - National Acad Sciences
Influenza A and B viruses contain proton-selective ion channels, A/M2 and BM2,
respectively, and the A/M2 channel activity is inhibited by the drugs amantadine and its …
respectively, and the A/M2 channel activity is inhibited by the drugs amantadine and its …
Folding and stability of α-helical integral membrane proteins
KR MacKenzie - Chemical reviews, 2006 - ACS Publications
Integral membrane proteins are embedded in a watersolvated lipid bilayer that presents
contrasting features in an anisotropic, chemically heterogeneous environment. A …
contrasting features in an anisotropic, chemically heterogeneous environment. A …
Total chemical synthesis of the integral membrane protein influenza A virus M2: role of its C-terminal domain in tetramer assembly
GG Kochendoerfer, D Salom, JD Lear… - Biochemistry, 1999 - ACS Publications
The M2 protein from influenza A virus is a 97-residue homotetrameric membrane protein that
functions as a proton channel. To determine the features required for the assembly of this …
functions as a proton channel. To determine the features required for the assembly of this …