ArticleBiophysical journal2010
Residue-specific side-chain packing determines the backbone dynamics of transmembrane model helices.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Conformational Flexibility of Transmembrane Helices: How it Works and Where it Matters.Chemical reviews · 2026Review
- Predicting peptide orientation in membrane interactions: a review on transmembrane and surface-bound states.European biophysics journal : EBJ · 2026Review
- Charting γ-secretase substrates by explainable AI.Nature communications · 2025Article
- AAclust:Bioinformatics advances · 2024Article
- Cooperation of N- and C-terminal substrate transmembrane domain segments in intramembrane proteolysis by γ-secretase.Communications biology · 2023Article
- Article
- Non-canonical Shedding of TNFα by SPPL2a Is Determined by the Conformational Flexibility of Its Transmembrane Helix.iScience · 2020Article
- Article
- Experimental determination and data-driven prediction of homotypic transmembrane domain interfaces.Computational and structural biotechnology journal · 2020Article
- Increased H-Bond Stability Relates to Altered ε-Cleavage Efficiency and Aβ Levels in the I45T Familial Alzheimer's Disease Mutant of APP.Scientific reports · 2019Article
- Dissecting conformational changes in APP's transmembrane domain linked to ε-efficiency in familial Alzheimer's disease.PloS one · 2018Article
- Expression, Functional Characterization, and Solid-State NMR Investigation of the G Protein-Coupled GHS Receptor in Bilayer Membranes.Scientific reports · 2017Article
- Article
- Herpesvirus gB: A Finely Tuned Fusion Machine.Viruses · 2015Review
- The backbone dynamics of the amyloid precursor protein transmembrane helix provides a rationale for the sequential cleavage mechanism of γ-secretase.Journal of the American Chemical Society · 2013Article
- Large extent of disorder in Adenomatous Polyposis Coli offers a strategy to guard Wnt signalling against point mutations.PloS one · 2013Article
- Sequence-dependent backbone dynamics of a viral fusogen transmembrane helix.Protein science : a publication of the Protein Society · 2012Article
- Shifting hydrogen bonds may produce flexible transmembrane helices.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Designing disorder: Tales of the unexpected tails.Intrinsically disordered proteinsReview
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6 authors.
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Abstract
The transmembrane domains (TMDs) of membrane-fusogenic proteins contain an overabundance of β-branched residues. In a previous effort to systematically study the relation among valine content, fusogenicity, and helix dynamics, we developed model TMDs that we termed LV-peptides. The content and position of valine in LV-peptides determine their fusogenicity and backbone dynamics, as shown experimentally. Here, we analyze their conformational dynamics and the underlying molecular forces using molecular-dynamics simulations. Our study reveals that backbone dynamics is correlated with the efficiency of side-chain to side-chain van der Waals packing between consecutive turns of the helix. Leu side chains rapidly interconvert between two rotameric states, thus favoring contacts to its i±3 and i±4 neighbors. Stereochemical restraints acting on valine side chains in the α-helix force both β-substituents into an orientation where i,i±3 interactions are less favorable than i,i±4 interactions, thus inducing a local packing deficiency at VV3 motifs. We provide a quantitative molecular model to explain the relationship among chain connectivity, side-chain mobility, and backbone flexibility. We expect that this mechanism also defines the backbone flexibility of natural TMDs.
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