A model of dynamic side-chain--side-chain interactions in the alpha-lactalbumin molten globule

scientific article

A model of dynamic side-chain--side-chain interactions in the alpha-lactalbumin molten globule is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1110/PS.34101
P932PMC publication ID2249850
P698PubMed publication ID11266594
P5875ResearchGate publication ID12065628

P50authorJianxing SongQ37375660
P2093author name stringL Luo
P Bai
Z Y Peng
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Rapid formation of a molten globule intermediate in refolding of alpha-lactalbuminQ28306450
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A test of the "jigsaw puzzle" model for protein folding by multiple methionine substitutions within the core of T4 lysozymeQ33367870
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-lactalbuminQ34288348
The solution structure of the DNA-binding domain of Skn-1Q36197947
Hydrophobic sequence minimization of the alpha-lactalbumin molten globuleQ36810158
Specificity of native-like interhelical hydrophobic contacts in the apomyoglobin intermediate.Q37168151
SKN-1 domain folding and basic region monomer stabilization upon DNA bindingQ37367381
Active barnase variants with completely random hydrophobic coresQ37593060
Thermal unfolding of human high-density apolipoprotein A-1: implications for a lipid-free molten globular stateQ37682995
Expression of a synthetic gene encoding canine milk lysozyme in Escherichia coli and characterization of the expressed proteinQ38323973
Three-state denaturation of α-lactalbumin by guanidine hydrochlorideQ39118524
Molten globule and protein foldingQ40944932
Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate: a comparative study of the folding reactions of alpha-lactalbumin and lysozymeQ41478567
The role of internal packing interactions in determining the structure and stability of a proteinQ44077439
A specific hydrophobic core in the alpha-lactalbumin molten globuleQ47885497
Contribution of individual residues to formation of the native-like tertiary topology in the alpha-lactalbumin molten globuleQ47885507
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. WrightQ57889918
Alternative packing arrangements in the hydrophobic core of λrepresserQ59096694
A 'molten-globule' membrane-insertion intermediate of the pore-forming domain of colicin AQ68065183
Strategy for analysing the co-operativity of intramolecular interactions in peptides and proteinsQ68891112
Characterization of a partly folded protein by NMR methods: studies on the molten globule state of guinea pig alpha-lactalbuminQ69585453
Comparison of the transient folding intermediates in lysozyme and alpha-lactalbuminQ70105070
Structure and dynamics of the acid-denatured molten globule state of alpha-lactalbumin: a two-dimensional NMR studyQ70576073
Packing interactions in the apomyglobin folding intermediateQ71031209
An empirical approach to protein conformation stability and flexibilityQ71205229
Following protein folding in real time using NMR spectroscopyQ71726951
The unfolding thermodynamics of c-type lysozymes: a calorimetric study of the heat denaturation of equine lysozymeQ71751606
A protein dissection study of a molten globuleQ72266488
Partially folded states of equine lysozyme. Structural characterization and significance for protein foldingQ72551818
Characterization of millisecond time-scale dynamics in the molten globule state of alpha-lactalbumin by NMRQ73301740
Side chain accessibility and dynamics in the molten globule state of alpha-lactalbumin: a (19)F-NMR studyQ73344601
Hydrogen exchange study of canine milk lysozyme: stabilization mechanism of the molten globuleQ74015797
P433issue1
P407language of work or nameEnglishQ1860
P304page(s)55-62
P577publication date2001-01-01
P1433published inProtein ScienceQ7251445
P1476titleA model of dynamic side-chain--side-chain interactions in the alpha-lactalbumin molten globule
P478volume10

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cites work (P2860)
Q43849838Characterization of a partially folded intermediate of stem bromelain at low pH.
Q74518042Fast compaction of alpha-lactalbumin during folding studied by stopped-flow X-ray scattering
Q35180679Independent 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
Q33411160Insight into "insoluble proteins" with pure water
Q28471978Insights into protein aggregation by NMR characterization of insoluble SH3 mutants solubilized in salt-free water

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