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• W2024463165 abstract "We have employed two-dimensional solid-state NMR to study structure and dynamics of insoluble folding states of the domain-swapped protein Crh. Starting from the protein precipitated at its pI, conformational changes due to a modest temperature increase were investigated at the level of individual residues and in real-time. As compared to the crystalline state, Crh pI-precipitates exhibited a higher degree of molecular mobility for several regions of the protein. A rigidly intact center was observed including a subset of residues of the hydrophobic core. Raising the temperature by 13 K to 282 K created a partially unfolded intermediate state that was converted into β-sheet-rich aggregates that are mostly of spherical character according to electron microscopy. Residue-by-residue analysis indicated that two out of three α-helices in aggregated Crh underwent major structural rearrangements while the third helix was preserved. Residues in the hinge region exhibited major chemical-shift changes, indicating that the domain swap was not conserved in the aggregated form. Our study provides direct evidence that protein aggregates of a domain-swapped protein retain a significant fraction of native secondary structure and demonstrates that solid-state NMR can be used to directly monitor slow molecular folding events." @default.
• W2024463165 created "2016-06-24" @default.
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• W2024463165 date "2006-12-15" @default.
• W2024463165 modified "2023-09-25" @default.
• W2024463165 title "Characterization of Folding Intermediates of a Domain-Swapped Protein by Solid-State NMR Spectroscopy" @default.
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• W2024463165 doi "https://doi.org/10.1021/ja066469x" @default.
• W2024463165 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17199296" @default.
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