| scholarly article | Q13442814 |
| P356 | DOI | 10.1007/BF00256531 |
| P2888 | exact match | https://scigraph.springernature.com/pub.10.1007/bf00256531 |
| P698 | PubMed publication ID | 3843533 |
| P50 | author | Dmitry Dolgikh | Q51037664 |
| P2093 | author name string | V E Bychkova | |
| G V Semisotnov | |||
| O B Ptitsyn | |||
| I A Bolotina | |||
| E I Tiktopulo | |||
| L V Abaturov | |||
| E V Brazhnikov | |||
| Lebedev YuO | |||
| R I Gilmanshin | |||
| P2860 | cites work | Polarization of the fluorescence of macromolecules. I. Theory and experimental method | Q24531310 |
| Protein Denaturation | Q34221155 | ||
| ‘Molten‐globule state’: a compact form of globular proteins with mobile side‐chains | Q34255230 | ||
| Oxidized RNase as a protein model having no contribution to the hydrogen exchange rate from conformational restrictions | Q35978743 | ||
| Electrophoretic investigations of the acid conformational change of alpha-lactalbumin | Q39064134 | ||
| Equilibrium and kinetics of the unfolding of α-lactalbumin by guanidine hydrochloride (II) | Q39087027 | ||
| Three-state denaturation of α-lactalbumin by guanidine hydrochloride | Q39118524 | ||
| Effect of inter-subunit contact on intramolecular conformational motility (conformational stability) of hemoglobin as revealed by hydrogen exchange | Q39121956 | ||
| Equilibrium and kinetics of the thermal unfolding of α-lactalbumin. The relation to its folding mechanism | Q39207434 | ||
| Detection of an early intermediate in the folding of ribonuclease A by protection of amide protons against exchange | Q39297679 | ||
| Stability of proteins: small globular proteins | Q39303667 | ||
| Hydrogen exchange | Q39919670 | ||
| Thermodynamic characterization of partially denatured states in the denaturation process of bovine α-lactalbumin by inorganic denaturants | Q40104777 | ||
| Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding | Q40130917 | ||
| Intensities and other spectral parameters of infrared amide bands of polypeptides in the ?- and random forms | Q42080800 | ||
| Denaturation of bovine carbonic anhydrase B by guanidine hydrochloride. A process involving separable sequential conformational transitions. | Q43423163 | ||
| Structure of α-lactalbumin and its fluctuation | Q44841058 | ||
| Comparative fluorescence properties of bovine, goat, human and guinea pig alpha lactalbumin. Characterization of the environments of individual tryptophan residues in partially folded conformers | Q46423954 | ||
| Growth hormone conformation and conformational equilibria. | Q47827797 | ||
| Estimation of globular protein secondary structure from circular dichroism. | Q51259487 | ||
| Folding of ribonuclease A from a partially disordered conformation. Kinetic study under folding conditions. | Q52714052 | ||
| Primary structure effects on peptide group hydrogen exchange. | Q52994305 | ||
| Use of small-angle x-ray scattering to determine protein conformation | Q53000660 | ||
| Acid denaturation of bovine carbonic anhydrase B. | Q64914053 | ||
| Estimation of amino acid residue side-chain absorption in the infrared spectra of protein solutions in heavy water | Q66965932 | ||
| Joint use of light, x‐ray and neutron scattering for investigation of RNA and protein mutual distribution within the 50S subparticle of E. coli ribosomes | Q67384571 | ||
| Detection and characterization of the intermediate on the folding pathway of human alpha-lactalbumin | Q67389493 | ||
| Evidence from rotatory measurement for intermediate state in the guanidine hydrochloride denaturation of beta-lactoglobulin | Q67598821 | ||
| A folding model of alpha-lactalbumin deduced from the three-state denaturation mechanism | Q67686751 | ||
| Intensities and other spectral parameters of infrared amide bands of polypeptides in the alpha-helical form | Q68791748 | ||
| Stages in the mechanism of self-organization of protein molecules | Q69556345 | ||
| [Acid form of carbonic anhydrase: "molten globule" with a secondary structure] | Q70458781 | ||
| 'Molten-globule' state accumulates in carbonic anhydrase folding | Q70462566 | ||
| [The theory of cooperative transitions in protein globules] | Q70540296 | ||
| Inter- and intramolecular interactions of alpha-lactalbumin. X. Effect of acylation of tyrosyl and lysyl side chains on molecular conformations | Q70554531 | ||
| Spectral evidence for a rapidly formed structural intermediate in the refolding kinetics of hen egg-white lysozyme | Q70753939 | ||
| Thermodynamics of alpha-lactalbumin unfolding | Q70865419 | ||
| Characteristics of the binding of Ca2+ and other divalent metal ions to bovine alpha-lactalbumin | Q70875471 | ||
| Role of the Interaction between Ionizable Groups in the Folding of Bovine α-Lactalbumin1 | Q70945346 | ||
| Alpha-Lactalbumin: compact state with fluctuating tertiary structure? | Q71064817 | ||
| alpha-Lactalbumin: a calcium metalloprotein | Q71517374 | ||
| Multiparameter kinetic study on the unfolding and refolding of bovine carbonic anhydrase B | Q71520227 | ||
| Molecular conformation of egg-white lysozyme and bovine α-lactalbumin in solution | Q71547142 | ||
| Calcium binding to alpha-lactalbumin: structural rearrangement and association constant evaluation by means of intrinsic protein fluorescence changes | Q71561639 | ||
| alpha-Lactalbumin binds magnesium ions: study by means of intrinsic fluorescence technique | Q71577030 | ||
| Circular dichroism spectra of α-lactalbumin | Q71617907 | ||
| On the column chromatography of bovine whey proteins | Q71672071 | ||
| The complete amino acid sequence of bovine alpha-lactalbumin | Q71730608 | ||
| Interactions of divalent metal ions with bovine, human, and goat alpha-lactalbumins | Q71829427 | ||
| Unfolding and refolding of Staphylococcus aureus penicillinase by urea-gradient electrophoresis | Q72093367 | ||
| Inter- and intramolecular interactions of alpha-lactalbumin. 8. The alkaline conformational change | Q72279608 | ||
| On the fractionation of β-lactoglobulin and α-lactalbumin | Q72293204 | ||
| On the systematic arrangement of molecules of "soluble" ribonucleic acid in aqueous solutions | Q72637431 | ||
| Kinetic study of protein unfolding and refolding using urea gradient electrophoresis | Q72847504 | ||
| Structural intermediates trapped during the folding of ribonuclease A by amide proton exchange | Q72881712 | ||
| A native-like intermediate on the ribonuclease A folding pathway. 2. Comparison of its properties to native ribonuclease A | Q72886681 | ||
| Inter- and intramolecular interactions of alpha-lactlabumin. VI. Optical rotation dispersion properties | Q72911010 | ||
| INTER- AND INTRAMOLECULAR INTERACTIONS OF ALPHA-LACTALBUMIN. II. AGGREGATION REACTIONS AT ACID PH | Q76988093 | ||
| INTER-AND INTRAMOLECULAR INTERACTIONS OF ALPHA-LACTALBUMIN. 3. SPECTRAL CHANGES AT ACID PH | Q78430647 | ||
| INTER- AND INTRAMOLECULAR INTERACTIONS OF ALPHA-LACTALBUMIN. IV. LOCATION OF TRYPTOPHAN GROUPS | Q78430652 | ||
| THE THEORY OF HELIX-COIL TRANSITIONS IN MACROMOLECULES | Q78526630 | ||
| Osmometry and general characterization of alpha-lactalbumin | Q79105555 | ||
| P433 | issue | 2 | |
| P304 | page(s) | 109-121 | |
| P577 | publication date | 1985-01-01 | |
| P1433 | published in | European Biophysics Journal | Q5412316 |
| P1476 | title | Compact state of a protein molecule with pronounced small-scale mobility: bovine alpha-lactalbumin | |
| P478 | volume | 13 |
| Q49852466 | "Cooperative collapse" of the denatured state revealed through Clausius-Clapeyron analysis of protein denaturation phase diagrams. |
| Q67593817 | 'All-or-none' mechanism of the molten globule unfolding |
| Q27636798 | A cavity-forming mutation in insulin induces segmental unfolding of a surrounding α-helix |
| Q43057928 | A comparative study of the alpha-subdomains of bovine and human alpha-lactalbumin reveals key differences that correlate with molten globule stability |
| Q91765309 | A look back at the molten globule state of proteins: thermodynamic aspects |
| Q42859757 | A three-disulphide derivative of hen lysozyme. Structure, dynamics and stability |
| Q73174198 | All-or-none solvent-induced transitions between native, molten globule and unfolded states in globular proteins |
| Q54714787 | An early immunoreactive folding intermediate of the tryptophan synthease beta 2 subunit is a 'molten globule'. |
| Q69422018 | An early intermediate of refolding alpha-lactalbumin forms within 20 ms |
| Q72347294 | Bipartite structure of the alpha-lactalbumin molten globule |
| Q44523618 | Characterization of molten globule state of fetuin at low pH. |
| Q42846760 | Compactness of the kinetic molten globule of bovine alpha-lactalbumin: a dynamic light scattering study |
| Q37727618 | Compressibility as a means to detect and characterize globular protein states |
| Q58322027 | Cooperative thermal transitions of bovine and human apo-α-lactalbumins: evidence for a new intermediate state |
| Q37924786 | Deuterium labelling in NMR structural analysis of larger proteins |
| Q44624197 | Differences in the Unfolding of Procerain Induced by pH, Guanidine Hydrochloride, Urea, and Temperature |
| Q35113283 | Distribution, transition and thermodynamic stability of protein conformations in the denaturant-induced unfolding of proteins |
| Q41972010 | Effect of hydrostatic pressure on unfolding of alpha-lactalbumin: volumetric equivalence of the molten globule and unfolded state |
| Q28361369 | Effects of i-propanol on the structural dynamics of Thermomyces lanuginosa lipase revealed by tryptophan fluorescence |
| Q50525064 | Evidence of molten globule like state(s) of interferon gamma in acidic and sodium perchlorate solutions. |
| Q32124440 | Exploration of partially unfolded states of human alpha-lactalbumin by molecular dynamics simulation |
| Q34186956 | HAMLET kills tumor cells by an apoptosis-like mechanism--cellular, molecular, and therapeutic aspects |
| Q37191846 | How does protein synthesis give rise to the 3D-structure? |
| Q68360957 | Hydrogen exchange of the tryptophan residues in bovine ?-lactalbumin studied by uv spectroscopy |
| Q36810158 | Hydrophobic sequence minimization of the alpha-lactalbumin molten globule |
| Q34989900 | Is polyproline II a major backbone conformation in unfolded proteins? |
| Q30423134 | Kinetics of interaction of partially folded proteins with a hydrophobic dye: evidence that molten globule character is maximal in early folding intermediates |
| Q59600481 | Local interactions and the role of the 6-120 disulfide bond in α-lactalbumin: implications for formation of the molten globule state |
| Q44827362 | Low concentration of guanidine hydrochloride induces the formation of an aggregation-prone state in alpha-urease |
| Q34130055 | Lysozyme and alpha-lactalbumin: structure, function, and interrelationships |
| Q30362403 | Membrane-induced changes in the holomyoglobin tertiary structure: interplay with function. |
| Q52535439 | Molecular dynamics simulations of human alpha-lactalbumin: changes to the structural and dynamical properties of the protein at low pH. |
| Q37770269 | Molten globule intermediates and protein folding |
| Q78099862 | Molten globule versus variety of intermediates: influence of anions on pH-denatured apomyoglobin |
| Q30354221 | NMR Spectroscopy and Protein Folding: Studies of Lysozyme and α-Lactalbumin |
| Q59086029 | NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A |
| Q52047122 | Native-like secondary structure of molten globules. |
| Q40261019 | Predissociated Dimers and Molten Globule Monomers in the Equilibrium Unfolding of Yeast Glutathione Reductase |
| Q37439424 | Probing early events in ferrous cytochrome c folding with time-resolved natural and magnetic circular dichroism spectroscopies |
| Q30427987 | Protein folding: the endgame |
| Q36591217 | Proteins unfold in steps |
| Q41812667 | Reduced BPTI is collapsed. A pulsed field gradient NMR study of unfolded and partially folded bovine pancreatic trypsin inhibitor |
| Q57136297 | Release of retinol and denaturation of its plasma carrier, retinol-binding protein |
| Q33883824 | Role of the molten globule state in protein folding. |
| Q36280575 | Solution structure of alpha t alpha, a helical hairpin peptide of de novo design |
| Q43058028 | Stability of HAMLET--a kinetically trapped alpha-lactalbumin oleic acid complex |
| Q41970859 | Structural and thermal stability analysis of Escherichia coli and Alicyclobacillus acidocaldarius thioredoxin revealed a molten globule-like state in thermal denaturation pathway of the proteins: an infrared spectroscopic study |
| Q40221852 | Structural basis for difference in heat capacity increments for Ca(2+) binding to two alpha-lactalbumins |
| Q53653268 | Structural characterisation of the human alpha-lactalbumin molten globule at high temperature. |
| Q42845790 | Structural characterization of the molten globule of alpha-lactalbumin by solution X-ray scattering |
| Q71940770 | The existence of a hexameric intermediate with molten-globule-like properties in the thermal denaturation of bovine-liver glutamate dehydrogenase |
| Q73897375 | The pH-dependent tertiary structure of a designed helix-loop-helix dimer |
| Q30431793 | The perturbations of the native state of goat alpha-lactalbumin induced by 1,1'-bis(4-anilino-5-naphthalenesulfonate) are Ca2+-dependent |
| Q34351283 | Transient folding intermediates characterized by protein engineering |
| Q31101954 | Truncated staphylococcal nuclease is compact but disordered |
| Q42222952 | Two steps in the transition between the native and acid states of bovine alpha-lactalbumin detected by circular polarization of luminescence: evidence for a premolten globule state? |
| Q30385084 | Understanding protein non-folding. |
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