| scholarly article | Q13442814 |
| P356 | DOI | 10.1016/J.JMB.2009.09.025 |
| P8608 | Fatcat ID | release_izdyfwa2szdhtds3q7564wiv7e |
| P932 | PMC publication ID | 2845811 |
| P698 | PubMed publication ID | 19766656 |
| P5875 | ResearchGate publication ID | 26824130 |
| P50 | author | Christina Redfield | Q40991351 |
| P2093 | author name string | Heike I Rösner | |
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| Intermediate states in protein folding | Q40990251 | ||
| Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate: a comparative study of the folding reactions of alpha-lactalbumin and lysozyme | Q41478567 | ||
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| Local and global cooperativity in the human alpha-lactalbumin molten globule | Q44819436 | ||
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| Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin | Q46929622 | ||
| A specific hydrophobic core in the alpha-lactalbumin molten globule | Q47885497 | ||
| Contribution of individual residues to formation of the native-like tertiary topology in the alpha-lactalbumin molten globule | Q47885507 | ||
| Proline scanning mutagenesis of a molten globule reveals non-cooperative formation of a protein's overall topology. | Q52520638 | ||
| Alpha-lactalbumin forms a compact molten globule in the absence of disulfide bonds. | Q54077167 | ||
| Folding pathway of Escherichia coli ribonuclease HI: a circular dichroism, fluorescence, and NMR study. | Q54598141 | ||
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| A residue-specific NMR view of the non-cooperative unfolding of a molten globule | Q57889932 | ||
| Complete resonance assignment for the polypeptide backbone of interleukin 1.beta. using three-dimensional heteronuclear NMR spectroscopy | Q57904897 | ||
| Equilibrium and Kinetic Studies on Folding of the Authentic and Recombinant Forms of Human α-Lactalbumin by Circular Dichroism Spectroscopy† | Q58840872 | ||
| pH-dependent stability of the human ?-lactalbumin molten globule state: Contrasting roles of the 6?120 disulfide and the ?-subdomain at low and neutral pH | Q59600477 | ||
| Calcium Binding Peptides from α-Lactalbumin: Implications for Protein Folding and Stability† | Q59600500 | ||
| Crystal structure of human α-lactalbumin at 1·7 Å resolution | Q60304615 | ||
| Structural characterization of a partly folded apomyoglobin intermediate | Q68568851 | ||
| Characterization of a partly folded protein by NMR methods: studies on the molten globule state of guinea pig alpha-lactalbumin | Q69585453 | ||
| Influence of Ca2+ binding on the structure and stability of bovine alpha-lactalbumin studied by circular dichroism and nuclear magnetic resonance spectra | Q70016691 | ||
| Structure and dynamics of the acid-denatured molten globule state of alpha-lactalbumin: a two-dimensional NMR study | Q70576073 | ||
| Disulfide determinants of calcium-induced packing in alpha-lactalbumin | Q70862469 | ||
| Alpha-Lactalbumin: compact state with fluctuating tertiary structure? | Q71064817 | ||
| Kinetic intermediates in the formation of the cytochrome c molten globule | Q71840986 | ||
| A protein dissection study of a molten globule | Q72266488 | ||
| Bipartite structure of the alpha-lactalbumin molten globule | Q72347294 | ||
| Characterization of millisecond time-scale dynamics in the molten globule state of alpha-lactalbumin by NMR | Q73301740 | ||
| Fast compaction of alpha-lactalbumin during folding studied by stopped-flow X-ray scattering | Q74518042 | ||
| P433 | issue | 2 | |
| P407 | language of work or name | English | Q1860 |
| P304 | page(s) | 351-362 | |
| P577 | publication date | 2009-09-18 | |
| P1433 | published in | Journal of Molecular Biology | Q925779 |
| P1476 | title | The human alpha-lactalbumin molten globule: comparison of structural preferences at pH 2 and pH 7. | |
| P478 | volume | 394 |
| Q37856774 | Conformation and thermodynamic stability of pre-molten and molten globule states of mammalian cytochromes-c |
| Q34329002 | High-throughput NMR assessment of the tertiary structure of food allergens |
| Q28487087 | Monomeric banana lectin at acidic pH overrules conformational stability of its native dimeric form |
| Q42945520 | Off-Pathway Status for the Alkali Molten Globule of Horse Ferricytochromec |
| Q48229352 | Ramachandran mapping of peptide conformation using a large database of computed Raman and Raman optical activity spectra. |
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