Literature DB >> 29789823

Influenza A M2 transmembrane domain tunes its conformational heterogeneity and structural plasticity in the lipid bilayer by forming loop structures.

Yue Liu1, Junjun Tan, Jiahui Zhang, Chuanzhao Li, Yi Luo, Shuji Ye.   

Abstract

We discovered for the first time that the influenza A virus M2TM tunes its conformational heterogeneity and structural plasticity to respond to environmental cues by undergoing a helix-to-loop transition, resolving controversies regarding the mechanism of proton conduction and plasticity of the M2TM in lipid bilayers.

Entities:  

Year:  2018        PMID: 29789823     DOI: 10.1039/c8cc01533c

Source DB:  PubMed          Journal:  Chem Commun (Camb)        ISSN: 1359-7345            Impact factor:   6.222


  3 in total

1.  Structure of von Willebrand factor A1 on polystyrene determined from experimental and calculated sum frequency generation spectra.

Authors:  Steven J Roeters; Elaine H Tronic; Joe E Baio; David G Castner; Tobias Weidner
Journal:  Biointerphases       Date:  2018-12-14       Impact factor: 2.456

2.  Otoferlin C2F Domain-Induced Changes in Membrane Structure Observed by Sum Frequency Generation.

Authors:  Thaddeus W Golbek; Murugesh Padmanarayana; Steven J Roeters; Tobias Weidner; Colin P Johnson; Joe E Baio
Journal:  Biophys J       Date:  2019-09-17       Impact factor: 4.033

3.  Ultrafast energy relaxation dynamics of amide I vibrations coupled with protein-bound water molecules.

Authors:  Junjun Tan; Jiahui Zhang; Chuanzhao Li; Yi Luo; Shuji Ye
Journal:  Nat Commun       Date:  2019-03-01       Impact factor: 14.919

  3 in total

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