ArticleBiophysical journal2008
Nonnative helical motif in a chaperone-bound protein fragment.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Critical Beginnings: Selective Tuning of Solubility and Structural Accuracy of Newly Synthesized Proteins by the Hsp70 Chaperone System.The journal of physical chemistry. B · 2023Article
- Protein folding in vitro and in the cell: From a solitary journey to a team effort.Biophysical chemistry · 2022Review
- Hsp70 molecular chaperones: multifunctional allosteric holding and unfolding machines.The Biochemical journal · 2019Review
- Article
- Hsp70 biases the folding pathways of client proteins.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Mapping the conformation of a client protein through the Hsp70 functional cycle.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Heterogeneous binding of the SH3 client protein to the DnaK molecular chaperone.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Transient interactions of a slow-folding protein with the Hsp70 chaperone machinery.Protein science : a publication of the Protein Society · 2012Article
- 1H-Detected 13C photo-CIDNP as a sensitivity enhancement tool in solution NMR.Journal of the American Chemical Society · 2011Article
- Confined dynamics of a ribosome-bound nascent globin: Cone angle analysis of fluorescence depolarization decays in the presence of two local motions.Protein science : a publication of the Protein Society · 2009Article
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2 authors.
Funding
Abstract
The effect of cotranslationally active chaperones on the conformation of incomplete protein chains is poorly understood. The secondary structure of a 77-residue chaperone-bound N-terminal protein fragment corresponding to the first five helices (A-E) of apomyoglobin (apoMb(1-77)) is investigated here at the residue-specific level by multidimensional NMR. The substrate-binding domain of DnaK, DnaK-beta, is employed as a chaperone model. By taking advantage of the improved spectral quality resulting from chaperone deuteration, we find that DnaK-beta-bound apoMb(1-77) displays a region of nonnative helicity at residues away from the main chaperone binding site. The nonnative structural motif comprises portions of the native D and E helices and has similar characteristics to the reported nonnative DE helical region of acid-unfolded full-length apoMb. Upon incorporation of the missing C-terminal amino acids, a structural kink develops between residues 56 and 57, and two separate native D and E helices are generated. This work highlights, for the first time to our knowledge, the presence of a nonnative helical motif in a large chaperone-bound protein fragment under physiologically relevant solution conditions.
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