ArticleProceedings of the National Academy of Sciences of the United States of America2005
Multiple subsets of side-chain packing in partially folded states of alpha-lactalbumins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Bladder cancer therapy using a conformationally fluid tumoricidal peptide complex.Nature communications · 2021Trial
- BAMLET administration via drinking water inhibits intestinal tumor development and promotes long-term health.Scientific reports · 2024Article
- The Cytoplasm-Entry Domain of Antibacterial CdiA Is a Dynamic α-Helical Bundle with Disulfide-Dependent Structural Features.Journal of molecular biology · 2019Article
- Mechanisms of amyloid formation revealed by solution NMR.Progress in nuclear magnetic resonance spectroscopy · 2015Review
- Heterogeneity of equilibrium molten globule state of cytochrome c induced by weak salt denaturants under physiological condition.PloS one · 2015Article
- Unfolding of a small protein proceeds via dry and wet globules and a solvated transition state.Biophysical journal · 2013Article
- Measurement of energy landscape roughness of folded and unfolded proteins.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Photophysics, photochemistry and energetics of UV light induced disulphide bridge disruption in apo-α-lactalbumin.Journal of fluorescence · 2012Article
- 1-Anilino-8-naphthalene sulfonate (ANS) is not a desirable probe for determining the molten globule state of chymopapain.PloS one · 2012Article
- Exploring tryptophan dynamics in acid-induced molten globule state of bovine alpha-lactalbumin: a wavelength-selective fluorescence approach.European biophysics journal : EBJ · 2010Article
- Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Refolding of ribonuclease A monitored by real-time photo-CIDNP NMR spectroscopy.Journal of biomolecular NMR · 2009Article
- Protein folding and unfolding studied at atomic resolution by fast two-dimensional NMR spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- A pre-existing hydrophobic collapse in the unfolded state of an ultrafast folding protein.Nature · 2007Article
- Intermediates: ubiquitous species on folding energy landscapes?Current opinion in structural biology · 2007Review
- BPPred: a Web-based computational tool for predicting biophysical parameters of proteins.Protein science : a publication of the Protein Society · 2007Article
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5 authors.
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Abstract
Photochemically induced dynamic nuclear polarization NMR pulse-labeling techniques have been used to obtain detailed information about side-chain surface accessibilities in the partially folded (molten globule) states of bovine and human alpha-lactalbumin prepared under a variety of well defined conditions. Pulse labeling involves generating nuclear polarization in the partially folded state, rapidly refolding the protein within the NMR sample tube, then detecting the polarization in the well dispersed native-state spectrum. Differences in the solvent accessibility of specific side chains in the various molten globule states indicate that the hydrophobic clusters involved in stabilizing the alpha-lactalbumin fold can be formed from interactions between a variety of different hydrophobic residues in both native and non-native environments. The multiple subsets of hydrophobic clusters are likely to result from the existence of distinct but closely related local minima on the free-energy landscape of the protein and show that the fold and topology of a given protein may be formed from degenerate groups of side chains.
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