scholarly journals Solid-State NMR Spectroscopy of the HIV gp41 Membrane Fusion Protein Supports Intermolecular Antiparallel β Sheet Fusion Peptide Structure in the Final Six-Helix Bundle State

2014 ◽  
Vol 426 (5) ◽  
pp. 1077-1094 ◽  
Author(s):  
Kelly Sackett ◽  
Matthew J. Nethercott ◽  
Zhaoxiong Zheng ◽  
David P. Weliky
Keyword(s):  
Solid State ◽  
Nmr Spectroscopy ◽  
Fusion Protein ◽  
Membrane Fusion ◽  
Solid State Nmr ◽  
Fusion Peptide ◽  
Peptide Structure ◽  
Helix Bundle ◽  
Membrane Fusion Protein ◽  
Β Sheet

Solid-State NMR Spectroscopy of Functional Amyloid from a Fungal Hydrophobin: A Well-Ordered β-Sheet Core Amidst Structural Heterogeneity

2012 ◽  
Vol 51 (50) ◽  
pp. 12621-12625 ◽  
Author(s):  
Vanessa K. Morris ◽  
Rasmus Linser ◽  
Karyn L. Wilde ◽  
Anthony P. Duff ◽  
Margaret Sunde ◽  
...  
Keyword(s):  
Solid State ◽  
Nmr Spectroscopy ◽  
Solid State Nmr ◽  
Structural Heterogeneity ◽  
Functional Amyloid ◽  
Solid State Nmr Spectroscopy ◽  
Β Sheet

Parallel β-Sheet Structure of Alanine Tetrapeptide in the Solid State As Studied by Solid-State NMR Spectroscopy

2016 ◽  
Vol 120 (34) ◽  
pp. 8932-8941 ◽  
Author(s):  
Tetsuo Asakura ◽  
Kumiko Horiguchi ◽  
Akihiro Aoki ◽  
Yugo Tasei ◽  
Akira Naito
Keyword(s):  
Solid State ◽  
Nmr Spectroscopy ◽  
Solid State Nmr ◽  
Solid State Nmr Spectroscopy ◽  
Sheet Structure ◽  
Β Sheet

scholarly journals Structural and Functional Properties of an Unusual Internal Fusion Peptide in a Nonenveloped Virus Membrane Fusion Protein

2004 ◽  
Vol 78 (6) ◽  
pp. 2808-2818 ◽  
Author(s):  
Maya Shmulevitz ◽  
Raquel F. Epand ◽  
Richard M. Epand ◽  
Roy Duncan
Keyword(s):  
Fusion Protein ◽  
Membrane Fusion ◽  
Fusion Proteins ◽  
Fusion Peptide ◽  
Loop Structure ◽  
Fusion Peptides ◽  
Enveloped Virus ◽  
Membrane Fusion Protein ◽  
Virus Fusion ◽  
Nonenveloped Virus

ABSTRACT The avian and Nelson Bay reoviruses are two of only a limited number of nonenveloped viruses capable of inducing cell-cell membrane fusion. These viruses encode the smallest known membrane fusion proteins (p10). We now show that a region of moderate hydrophobicity we call the hydrophobic patch (HP), present in the small N-terminal ectodomain of p10, shares the following characteristics with the fusion peptides of enveloped virus fusion proteins: (i) an abundance of glycine and alanine residues, (ii) a potential amphipathic secondary structure, (iii) membrane-seeking characteristics that correspond to the degree of hydrophobicity, and (iv) the ability to induce lipid mixing in a liposome fusion assay. The p10 HP is therefore predicted to provide a function in the mechanism of membrane fusion similar to those of the fusion peptides of enveloped virus fusion peptides, namely, association with and destabilization of opposing lipid bilayers. Mutational and biophysical analysis suggested that the internal fusion peptide of p10 lacks alpha-helical content and exists as a disulfide-stabilized loop structure. Similar kinked structures have been reported in the fusion peptides of several enveloped virus fusion proteins. The preservation of a predicted loop structure in the fusion peptide of this unusual nonenveloped virus membrane fusion protein supports an imperative role for a kinked fusion peptide motif in biological membrane fusion.

Efficient β-Sheet Identification in Proteins by Solid-State NMR Spectroscopy

2000 ◽  
Vol 122 (46) ◽  
pp. 11320-11327 ◽  
Author(s):  
Daniel Huster ◽  
Satoru Yamaguchi ◽  
Mei Hong
Keyword(s):  
Solid State ◽  
Nmr Spectroscopy ◽  
Solid State Nmr ◽  
Solid State Nmr Spectroscopy ◽  
Β Sheet
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