ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2019
Stereochemistry of residues in turning regions of helical proteins.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed.
- Molecular Docking and Molecular Dynamics Simulations in Related toTropical medicine and infectious disease · 2023Review
- Conjecture on the Design of Helical Proteins.The journal of physical chemistry. B · 2020Article
- Structural stability of the SARS-CoV-2 main protease: Can metal ions affect function?Journal of inorganic biochemistry · 2020Article
- Unfolding cytochromes c-bJournal of inorganic biochemistry · 2020Article
- Funneled angle landscapes for helical proteins.Journal of inorganic biochemistry · 2020Article
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2 authors.
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Abstract
We have developed a geometrical approach to quantify differences in the stereochemistry of α-helical and turning regions in four iron proteins. Two spatial signatures are used to analyze residue coordinate data for each protein; and a third is employed to analyze amino-acid molecular volume data. The residue-by-residue analysis of the results, taken together with the finding that two major factors stabilize an α-helix (minimization of side-chain steric interference and intrachain H-bonding), lead to the conclusion that certain residues are preferentially selected for α-helix formation. In the sequential, de novo synthesis of a turning region, residues are preferentially selected such that the overall molecular volume profile (representing purely repulsive, excluded-volume effects) spans a small range Δ of values (Δ = 39.1 Å
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