ArticleProtein science : a publication of the Protein Society1999
Conformational properties of native sperm whale apomyoglobin in solution.
Article in Protein science : a publication of the Protein Society, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 52 citations in OpenAlex.
- Mapping Protein-Protein Interactions at Birth: Single-Particle Cryo-EM Analysis of a Ribosome-Nascent Globin Complex.ACS central science · 2024Article
- 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
- Real-time tracking of protein unfolding with time-resolved x-ray solution scattering.Structural dynamics (Melville, N.Y.) · 2020Article
- Complex Folding Landscape of Apomyoglobin at Acidic pH Revealed by Ultrafast Kinetic Analysis of Core Mutants.The journal of physical chemistry. B · 2018Article
- Replacement of the Distal Histidine Reveals a Noncanonical Heme Binding Site in a 2-on-2 Hemoglobin.Biochemistry · 2018Article
- How Does Your Protein Fold? Elucidating the Apomyoglobin Folding Pathway.Accounts of chemical research · 2017Article
- Kinetic intermediates of holo- and apo-myoglobin studied using HDX-TIMS-MS and molecular dynamic simulations.Journal of the American Society for Mass Spectrometry · 2015Article
- Probing the non-native H helix translocation in apomyoglobin folding intermediates.Biochemistry · 2014Article
- Mapping protein conformational heterogeneity under pressure with site-directed spin labeling and double electron-electron resonance.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Microsecond folding dynamics of apomyoglobin at acidic pH.The journal of physical chemistry. B · 2012Article
- Location trumps length: polyglutamine-mediated changes in folding and aggregation of a host protein.Biophysical journal · 2011Article
- Measurement of protein unfolding/refolding kinetics and structural characterization of hidden intermediates by NMR relaxation dispersion.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Folding mechanism of reduced Cytochrome c: equilibrium and kinetic properties in the presence of carbon monoxide.Journal of molecular biology · 2008Article
- Hierarchical folding mechanism of apomyoglobin revealed by ultra-fast H/D exchange coupled with 2D NMR.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Review
- Three-state protein folding: experimental determination of free-energy profile.Protein science : a publication of the Protein Society · 2005Article
- Enhanced picture of protein-folding intermediates using organic solvents in H/D exchange and quench-flow experiments.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Nonspecific hydrophobic interactions stabilize an equilibrium intermediate of apomyoglobin at a key position within the AGH region.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Modulation of the structural integrity of helix F in apomyoglobin by single amino acid replacements.Protein science : a publication of the Protein Society · 2004Article
- Photothermal studies of pH induced unfolding of apomyoglobin.Journal of protein chemistry · 2003Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Apomyoglobin from sperm whale is often used for studies of ligand binding, protein folding, and protein stability. In an effort to describe its conformational properties in solution, homonuclear and heteronuclear (13C and 15N) NMR methods were applied to the protein in its native state. Assignments were confirmed for nuclear Overhauser effects (NOEs) involving side chain and backbone protons in the folded regions of the structure. These NOEs were used to derive distance restraints. The shifts induced by the hydrophobic dye 8-anilino-1-naphthalenesulfonic acid (ANS) were inspected in the regions remote from its binding site and served as an indicator of conformational flexibility. 3JalphaH-NH values were obtained to assess dihedral angle averaging and to provide additional restraints. A family of structures was calculated with X-PLOR and an ab initio simulated annealing protocol using holomyoglobin as a template. Where the structure appeared well defined by chemical shift, line width, ANS perturbation, and density of NOEs, the low resolution model of apomyoglobin provides a valid approximation for the structure. The new model offers an improved representation of the folded regions of the protein, which encompass the A, B, E, helices as well as parts of the G and H helices. Regions that are less well defined at this stage of calculations include the CD corner and the end of the H-helix. The EF-F-FG segment remains uncharacterized.
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