scholarly article | Q13442814 |
P50 | author | Jianxing Song | Q37375660 |
P2093 | author name string | L Luo | |
P Bai | |||
Z Y Peng | |||
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Rapid formation of a molten globule intermediate in refolding of alpha-lactalbumin | Q28306450 | ||
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Protein structure prediction in the postgenomic era. | Q30326890 | ||
Mean-field minimization methods for biological macromolecules | Q30424576 | ||
A test of the "jigsaw puzzle" model for protein folding by multiple methionine substitutions within the core of T4 lysozyme | Q33367870 | ||
Role of the molten globule state in protein folding. | Q33883824 | ||
Different subdomains are most protected from hydrogen exchange in the molten globule and native states of human alpha-lactalbumin | Q34288348 | ||
The solution structure of the DNA-binding domain of Skn-1 | Q36197947 | ||
Hydrophobic sequence minimization of the alpha-lactalbumin molten globule | Q36810158 | ||
Specificity of native-like interhelical hydrophobic contacts in the apomyoglobin intermediate. | Q37168151 | ||
SKN-1 domain folding and basic region monomer stabilization upon DNA binding | Q37367381 | ||
Active barnase variants with completely random hydrophobic cores | Q37593060 | ||
Thermal unfolding of human high-density apolipoprotein A-1: implications for a lipid-free molten globular state | Q37682995 | ||
Expression of a synthetic gene encoding canine milk lysozyme in Escherichia coli and characterization of the expressed protein | Q38323973 | ||
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 | ||
The role of internal packing interactions in determining the structure and stability of a protein | Q44077439 | ||
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 | ||
Structural characterisation and comparison of the native and A-states of equine lysozyme. | Q50528369 | ||
Ligand binding is the principal determinant of stability for the p21(H)-ras protein. | Q52532232 | ||
Probing the molten globule state of alpha-lactalbumin by limited proteolysis. | Q54160128 | ||
The cytoplasmic fragment of the aspartate receptor displays globally dynamic behavior. | Q54590120 | ||
Local structural preferences in the alpha-lactalbumin molten globule. | Q54615586 | ||
Rapid collapse and slow structural reorganisation during the refolding of bovine α-lactalbumin 1 1Edited by P. E. Wright | Q57889918 | ||
Alternative packing arrangements in the hydrophobic core of λrepresser | Q59096694 | ||
A 'molten-globule' membrane-insertion intermediate of the pore-forming domain of colicin A | Q68065183 | ||
Strategy for analysing the co-operativity of intramolecular interactions in peptides and proteins | Q68891112 | ||
Characterization of a partly folded protein by NMR methods: studies on the molten globule state of guinea pig alpha-lactalbumin | Q69585453 | ||
Comparison of the transient folding intermediates in lysozyme and alpha-lactalbumin | Q70105070 | ||
Structure and dynamics of the acid-denatured molten globule state of alpha-lactalbumin: a two-dimensional NMR study | Q70576073 | ||
Packing interactions in the apomyglobin folding intermediate | Q71031209 | ||
An empirical approach to protein conformation stability and flexibility | Q71205229 | ||
Following protein folding in real time using NMR spectroscopy | Q71726951 | ||
The unfolding thermodynamics of c-type lysozymes: a calorimetric study of the heat denaturation of equine lysozyme | Q71751606 | ||
A protein dissection study of a molten globule | Q72266488 | ||
Partially folded states of equine lysozyme. Structural characterization and significance for protein folding | Q72551818 | ||
Characterization of millisecond time-scale dynamics in the molten globule state of alpha-lactalbumin by NMR | Q73301740 | ||
Side chain accessibility and dynamics in the molten globule state of alpha-lactalbumin: a (19)F-NMR study | Q73344601 | ||
Hydrogen exchange study of canine milk lysozyme: stabilization mechanism of the molten globule | Q74015797 | ||
P433 | issue | 1 | |
P407 | language of work or name | English | Q1860 |
P304 | page(s) | 55-62 | |
P577 | publication date | 2001-01-01 | |
P1433 | published in | Protein Science | Q7251445 |
P1476 | title | A model of dynamic side-chain--side-chain interactions in the alpha-lactalbumin molten globule | |
P478 | volume | 10 |
Q43849838 | Characterization of a partially folded intermediate of stem bromelain at low pH. |
Q74518042 | Fast compaction of alpha-lactalbumin during folding studied by stopped-flow X-ray scattering |
Q35180679 | Independent of their localization in protein the hydrophobic amino acid residues have no effect on the molten globule state of apomyoglobin and the disulfide bond on the surface of apomyoglobin stabilizes this intermediate state |
Q33411160 | Insight into "insoluble proteins" with pure water |
Q28471978 | Insights into protein aggregation by NMR characterization of insoluble SH3 mutants solubilized in salt-free water |
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