| scholarly article | Q13442814 |
| P819 | ADS bibcode | 2005PNAS..102.8899M |
| P356 | DOI | 10.1073/PNAS.0500661102 |
| P932 | PMC publication ID | 1157025 |
| P698 | PubMed publication ID | 15956205 |
| P5875 | ResearchGate publication ID | 7787048 |
| P50 | author | Peter Hore | Q7174733 |
| K Hun Mok | Q42167287 | ||
| Iain J. Day | Q42167301 | ||
| P2093 | author name string | Christopher M Dobson | |
| Toshio Nagashima | |||
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| Improved photo-CIDNP methods for studying protein structure and folding. | Q30326790 | ||
| Photo-CIDNP NMR methods for studying protein folding. | Q30342440 | ||
| Simultaneous determination of protein structure and dynamics. | Q30349988 | ||
| Probing protein structure by solvent perturbation of NMR spectra. Photochemically induced dynamic nuclear polarization and paramagnetic perturbation techniques applied to the study of the molten globule state of alpha-lactalbumin | Q30419189 | ||
| Rapid sample-mixing technique for transient NMR and photo-CIDNP spectroscopy: applications to real-time protein folding | Q30881731 | ||
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| Role of the molten globule state in protein folding. | Q33883824 | ||
| Three key residues form a critical contact network in a protein folding transition state | Q33935381 | ||
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| Molecular recognition. Conformational analysis of limited proteolytic sites and serine proteinase protein inhibitors | Q34787907 | ||
| Using nuclear magnetic resonance spectroscopy to study molten globule states of proteins | Q35850729 | ||
| Unfolded proteins and protein folding studied by NMR. | Q35860163 | ||
| Detection of residue contacts in a protein folding intermediate | Q36651008 | ||
| Hydrophobic sequence minimization of the alpha-lactalbumin molten globule | Q36810158 | ||
| Three-state denaturation of α-lactalbumin by guanidine hydrochloride | Q39118524 | ||
| Molten globule and protein folding | Q40944932 | ||
| 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 | ||
| Treatment of skin papillomas with topical alpha-lactalbumin-oleic acid | Q42629992 | ||
| P433 | issue | 25 | |
| P407 | language of work or name | English | Q1860 |
| P304 | page(s) | 8899-8904 | |
| P577 | publication date | 2005-06-13 | |
| P1433 | published in | Proceedings of the National Academy of Sciences of the United States of America | Q1146531 |
| P1476 | title | Multiple subsets of side-chain packing in partially folded states of alpha-lactalbumins | |
| P478 | volume | 102 |
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| Q37408309 | A pre-existing hydrophobic collapse in the unfolded state of an ultrafast folding protein |
| Q36420317 | BPPred: a Web-based computational tool for predicting biophysical parameters of proteins |
| Q34873055 | Can misfolded proteins be beneficial? The HAMLET case |
| Q27663290 | Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP |
| Q43107662 | Exploring tryptophan dynamics in acid-induced molten globule state of bovine alpha-lactalbumin: a wavelength-selective fluorescence approach |
| Q39222310 | Folding of proteins with a flavodoxin-like architecture |
| Q45130155 | Guanidine hydrochloride-induced alkali molten globule model of horse ferrocytochrome c. |
| Q30576410 | HAMLET: functional properties and therapeutic potential |
| Q35596344 | Heterogeneity of equilibrium molten globule state of cytochrome c induced by weak salt denaturants under physiological condition. |
| Q36713676 | Intermediates: ubiquitous species on folding energy landscapes? |
| Q36438472 | Measurement of energy landscape roughness of folded and unfolded proteins |
| Q26797492 | Mechanisms of amyloid formation revealed by solution NMR |
| Q58062013 | Nonequilibrium NMR Methods for Monitoring Protein and RNA Folding |
| Q42945520 | Off-Pathway Status for the Alkali Molten Globule of Horse Ferricytochromec |
| Q50524732 | Photophysics, photochemistry and energetics of UV light induced disulphide bridge disruption in apo-α-lactalbumin. |
| Q36090136 | Protein folding and unfolding studied at atomic resolution by fast two-dimensional NMR spectroscopy |
| Q42167126 | Refolding of ribonuclease A monitored by real-time photo-CIDNP NMR spectroscopy. |
| Q49967370 | Structural plasticity of the Salmonella FliS flagellar export chaperone |
| Q38269925 | The roughness of the protein energy landscape results in anomalous diffusion of the polypeptide backbone |
| Q51381718 | Thermodynamic analysis of ANS binding to partially unfolded α-lactalbumin: correlation of endothermic to exothermic changeover with formation of authentic molten globules. |
| Q37337994 | Unfolding of a small protein proceeds via dry and wet globules and a solvated transition state |
| Q40532568 | pH-dependence of single-protein adsorption and diffusion at a liquid chromatographic interface |
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