ArticleProceedings of the National Academy of Sciences of the United States of America2004
Nonspecific hydrophobic interactions stabilize an equilibrium intermediate of apomyoglobin at a key position within the AGH region.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed, 29 citations in OpenAlex.
- Influence of α-Helical Content on the Thermodiffusion of Apomyoglobin.Langmuir : the ACS journal of surfaces and colloids · 2025Article
- Characterization of molten globule PopB in absence and presence of its chaperone PcrH.The protein journal · 2012Article
- Site-specific hydration dynamics in the nonpolar core of a molten globule by dynamic nuclear polarization of water.Journal of the American Chemical Society · 2011Article
- Article
- Desolvation and development of specific hydrophobic core packing during Im7 folding.Journal of molecular biology · 2010Article
- How strong are side chain interactions in the folding intermediate?Protein science : a publication of the Protein Society · 2009Article
- Protein folding and misfolding: mechanism and principles.Quarterly reviews of biophysics · 2007Review
- Hydrophobic surface burial is the major stability determinant of a flat, single-layer beta-sheet.Journal of molecular biology · 2007Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Acid-induced unfolding of apomyoglobin (apoMb) proceeds in a multistate process involving at least one equilibrium intermediate (I) at pH 4.2. The structure of the I form has been investigated thoroughly, with significant effort devoted to identifying potentially stabilizing native contacts. Here, we test whether rigid side-chain packing interactions like those in holomyoglobin persist at a buried position, Met-131, within the low-pH apoMb intermediate. We have measured the urea-induced unfolding transitions of overpacking, underpacking, and polar substitutions of Met-131 to determine the effect on the stability of the native and intermediate states of apoMb. Whereas underpacking substitutions should destabilize the I form irrespective of the degree of native side-chain-packing interactions, we anticipate that overpacking replacements might show opposite effects in a tightly packed environment, compared with a region lacking native side-chain packing interactions. We observe that, whereas underpacking and polar substitutions destabilize the I form, overpacking substitutions are stabilizing, implying that I is structurally plastic. We also report a strong correlation between the I state unfolding free energies and side-chain transfer free energies from water to octanol. Our results suggest that, whereas side-chain hydrophobicity is important for the stability of the I form, specific side-chain packing interactions are not.
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