ArticleProtein science : a publication of the Protein Society2004
Modulation of the structural integrity of helix F in apomyoglobin by single amino acid replacements.
Article in Protein science : a publication of the Protein Society, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- 3D Proteomics: Structural, Functional, Chemical and Biomarker Discovery Proteomics With LiP-MS.Molecular & cellular proteomics : MCP · 2026Review
- Influence of α-Helical Content on the Thermodiffusion of Apomyoglobin.Langmuir : the ACS journal of surfaces and colloids · 2025Article
- Experimental methods to study the structure and dynamics of intrinsically disordered regions in proteins.Current research in structural biology · 2024Review
- Impact of A90P, F106L and H64V mutations on neuroglobin stability and ligand binding kinetics.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019Article
- Measuring protein structural changes on a proteome-wide scale using limited proteolysis-coupled mass spectrometry.Nature protocols · 2017Article
- Application of conventional molecular dynamics simulation in evaluating the stability of apomyoglobin in urea solution.Scientific reports · 2017Article
- Insights from molecular dynamics simulations for computational protein design.Molecular systems design & engineering · 2017Article
- Article
- Filling up the heme pocket stabilizes apomyoglobin and speeds up its folding.The journal of physical chemistry. B · 2014Article
- Article
- New protein footprinting: fast photochemical iodination combined with top-down and bottom-up mass spectrometry.Journal of the American Society for Mass Spectrometry · 2012Article
- Article
- Consequences of stabilizing the natively disordered f helix for the folding pathway of apomyoglobin.Journal of molecular biology · 2011Article
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7 authors.
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Abstract
The conformational features of native and mutant forms of sperm-whale apomyoglobin (apoMb) at neutral pH were probed by limited proteolysis experiments utilizing up to eight proteases of different substrate specificities. It was shown that all proteases selectively cleave apoMb at the level of chain segment 82-94 (HEAELKPLAQSHA), encompassing helix F in the X-ray structure of the holo form of the native protein; for example, thermolysin cleaves the Pro 88-Leu 89 peptide bond. These results indicate that helix F is highly flexible or largely disrupted in apoMb. Because helix F contains the helix-breaking Pro 88 residue, we propose that helix F is kept in place in the native holo protein by a variety of helix-heme stabilizing interactions. To modulate the stability of helix F, the Pro88Ala and Pro88Gly mutants were prepared by site-directed mutagenesis, and their conformational properties investigated by both far-UV circular dichroism spectroscopy and limited proteolysis. The helix content of the Pro88Ala mutant was somewhat enhanced with respect to that of both native and Pro88Gly mutant, as expected from the fact that Ala is the strongest helix inducer among the 20 amino acid residues. The rate of limited proteolysis of the three apoMb variants by thermolysin and proteinase K was in the order native > Pro88Gly >> Pro88Ala, in agreement with the scale of helix propensity of Ala, Gly, and Pro. The possible role of the flexible/unfolded chain segment 82-94 for the function and fate of apoMb at the cellular level is discussed.
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