ArticleBiophysical journal2007
The distribution of residues in a polypeptide sequence is a determinant of aggregation optimized by evolution.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 60 citations in OpenAlex.
- Order of amino acid recruitment into the genetic code resolved by last universal common ancestor's protein domains.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Order of amino acid recruitment into the genetic code resolved by Last Universal Common Ancestor's protein domains.bioRxiv : the preprint server for biology · 2024Article
- A3D Model Organism Database (A3D-MODB): a database for proteome aggregation predictions in model organisms.Nucleic acids research · 2024Article
- Sequence Versus Composition: What Prescribes IDP Biophysical Properties?Entropy (Basel, Switzerland) · 2019Article
- A Shift in Aggregation Avoidance Strategy Marks a Long-Term Direction to Protein Evolution.Genetics · 2019Article
- Theory of Sequence Effects in Amyloid Aggregation.The journal of physical chemistry. B · 2018Article
- Article
- Effect of position-specific single-point mutations and biophysical characterization of amyloidogenic peptide fragments identified from lattice corneal dystrophy patients.The Biochemical journal · 2017Article
- Antibody Aggregation: Insights from Sequence and Structure.Antibodies (Basel, Switzerland) · 2016Review
- Comparison of the aggregation of homologous β2-microglobulin variants reveals protein solubility as a key determinant of amyloid formation.Journal of molecular biology · 2016Article
- Computational analysis of candidate prion-like proteins in bacteria and their role.Frontiers in microbiology · 2015Article
- Misfolding and amyloid aggregation of apomyoglobin.International journal of molecular sciences · 2013Review
- Analyses of the general rule on residue pair frequencies in local amino acid sequences of soluble, ordered proteins.Protein science : a publication of the Protein Society · 2013Article
- On the role of aggregation prone regions in protein evolution, stability, and enzymatic catalysis: insights from diverse analyses.PLoS computational biology · 2013Article
- Resolution of the effects induced by W → F substitutions on the conformation and dynamics of the amyloid-forming apomyoglobin mutant W7FW14F.European biophysics journal : EBJ · 2012Article
- An evolutionary trade-off between protein turnover rate and protein aggregation favors a higher aggregation propensity in fast degrading proteins.PLoS computational biology · 2011Article
- Proline periodicity modulates the self-assembly properties of elastin-like polypeptides.The Journal of biological chemistry · 2010Article
- Potential aggregation-prone regions in complementarity-determining regions of antibodies and their contribution towards antigen recognition: a computational analysis.Pharmaceutical research · 2010Article
- Article
- NetCSSP: web application for predicting chameleon sequences and amyloid fibril formation.Nucleic acids research · 2009Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
It has been shown that the propensity of a protein to form amyloid-like fibrils can be predicted with high accuracy from the knowledge of its amino acid sequence. It has also been suggested, however, that some regions of the sequences are more important than others in determining the aggregation process. Here, we have addressed this issue by constructing a set of "sequence scrambled" variants of the first 29 residues of horse heart apomyoglobin (apoMb(1-29)), in which the sequence was modified while maintaining the same amino acid composition. The clustering of the most amyloidogenic residues in one region of the sequence was found to cause a marked increase of the elongation rate (k(agg)) and a remarkable shortening of the lag phase (t(lag)) of the fibril growth, as determined by far-UV circular dichroism and thioflavin T fluorescence. We also show that taking explicitly into consideration the presence of aggregation-promoting regions in the predictive methods results in a quantitative agreement between the theoretical and observed k(agg) and t(lag) values of the apoMb(1-29) variants. These results, together with a comparison between homologous segments from the family of globins, indicate the existence of a negative selection against the clustering of highly amyloidogenic residues in one or few regions of polypeptide sequences.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.