Related ArticlesStructure and dynamics of the acid-denatured molten globule state of alpha-lactalbumin: a two-dimensional NMR study.
Biochemistry. 1993 Feb 23;32(7):1707-18
Authors: Alexandrescu AT, Evans PA, Pitkeathly M, Baum J, Dobson CM
Two-dimensional 1H-NMR spectroscopy has been used to study the acid-denatured molten globule (A-state) of alpha-lactalbumin. The NMR spectra show that chemical shift dispersion is limited but significantly greater than that expected for a random coil conformation. The small chemical shift dispersion of side-chain resonances in the A-state together with line broadening associated with conformational averaging indicates that most of the long-range tertiary structure in the A-state is likely to be nonspecific. Side-chain resonances in the A-state are generally shifted somewhat upfield of random coil values; this and the observation of a large number of interresidue NOEs, however, indicate that some side-chain interactions, at least at the level of hydrophobic clustering, exist in the A-state. Analysis of NOESY spectra shows no evidence for an ordered structure for either of the two major clusters of aromatic residues which in the native structure make up part of the hydrophobic core of the helical domain of the native protein. A new aromatic cluster in the A-state which results from rearrangement of the side chains of Tyr103, Trp104, and His107 from their native state positions was, however, detected by a number of well-defined interresidue NOE effects. Similar NOE patterns are observed in a peptide corresponding to residues 101-110 of alpha-lactalbumin in trifluoroethanol, suggesting that the non-native structure in the 101-110 region of the A-state is not dependent on specific interactions with the rest of the chain. Trapping experiments indicate that amide protons from regions of the sequence which in the native state are helical are among those strongly protected from solvent exchange in the A-state; those from one of the helices (the C helix) were specifically identified. Taken together, these results reinforce a model of the A-state which has stable regions of localized secondary structure but a largely disordered tertiary structure.
[NMR paper] Water-protein interactions in the molten-globule state of carbonic anhydrase b: an NM
Water-protein interactions in the molten-globule state of carbonic anhydrase b: an NMR spin-diffusion study.
Related Articles Water-protein interactions in the molten-globule state of carbonic anhydrase b: an NMR spin-diffusion study.
Protein Sci. 2000 Aug;9(8):1540-7
Authors: Kutyshenko VP, Cortijo M
We have used the homonuclear Overhauser effect (NOE) to characterize a model protein: carbonic anhydrase B. We have obtained NOE difference spectra for this protein, centering the on-resonance signals either at the methyl-proton or at the...
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[NMR paper] Side chain accessibility and dynamics in the molten globule state of alpha-lactalbumi
Side chain accessibility and dynamics in the molten globule state of alpha-lactalbumin: a (19)F-NMR study.
Related Articles Side chain accessibility and dynamics in the molten globule state of alpha-lactalbumin: a (19)F-NMR study.
Biochemistry. 2000 Jan 18;39(2):372-80
Authors: Bai P, Luo L, Peng Z
The molten globule state of alpha-lactalbumin (alpha-LA) has been considered a prototype of partially folded proteins. Despite the importance of molten globules in understanding the mechanisms of protein folding and its relevance to some biological...
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[NMR paper] Structural characterization of the molten globule and native states of ovalbumin: a 1
Structural characterization of the molten globule and native states of ovalbumin: a 1H NMR study.
Related Articles Structural characterization of the molten globule and native states of ovalbumin: a 1H NMR study.
J Pept Res. 1997 Dec;50(6):465-74
Authors: Sogami M, Era S, Koseki T, Nagai N
Molecular characteristics of ovalbumin (OVA) in the acidic (pD 3.08, the E-form) and neutral regions were studied by measuring effective radii, 1H NMR spectra, spin-echo 1H NMR spectra and cross-relaxation times (TIS) from irradiated to observed protein...
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[NMR paper] Populating the equilibrium molten globule state of apomyoglobin under conditions suit
Populating the equilibrium molten globule state of apomyoglobin under conditions suitable for structural characterization by NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Populating the equilibrium molten globule state of apomyoglobin under conditions suitable for structural characterization by NMR.
FEBS Lett. 1997 Nov 3;417(1):92-6
Authors: Eliezer D, Jennings PA, Dyson HJ, Wright PE
Conditions have been determined under which the equilibrium molten globule...
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[NMR paper] A residue-specific NMR view of the non-cooperative unfolding of a molten globule.
A residue-specific NMR view of the non-cooperative unfolding of a molten globule.
Related Articles A residue-specific NMR view of the non-cooperative unfolding of a molten globule.
Nat Struct Biol. 1997 Aug;4(8):630-4
Authors: Schulman BA, Kim PS, Dobson CM, Redfield C
Molten globules are partially folded forms of proteins that are thought to be general intermediates in protein folding. Nonetheless, there is limited structural information about such species because they possess conformational heterogeneity and complex dynamical properties that...
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[NMR paper] Is apomyoglobin a molten globule? Structural characterization by NMR.
Is apomyoglobin a molten globule? Structural characterization by NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Is apomyoglobin a molten globule? Structural characterization by NMR.
J Mol Biol. 1996 Nov 8;263(4):531-8
Authors: Eliezer D, Wright PE
Multi-dimensional heteronuclear NMR spectroscopy has been used to obtain structural information on isotopically labeled recombinant sperm whale apomyoglobin in the native state at pH 6.1. Assignments for backbone...
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[NMR paper] Stability of alpha-helices in a molten globule state of cytochrome c by hydrogen-deut
Stability of alpha-helices in a molten globule state of cytochrome c by hydrogen-deuterium exchange and two-dimensional NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Stability of alpha-helices in a molten globule state of cytochrome c by hydrogen-deuterium exchange and two-dimensional NMR spectroscopy.
J Mol Biol. 1995 Apr 7;247(4):682-8
Authors: Kuroda Y, Endo S, Nagayama K, Wada A
To distinguish between intrinsically stable helices and those...
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[NMR paper] Structure and dynamics of a denatured 131-residue fragment of staphylococcal nuclease
Structure and dynamics of a denatured 131-residue fragment of staphylococcal nuclease: a heteronuclear NMR study.
Related Articles Structure and dynamics of a denatured 131-residue fragment of staphylococcal nuclease: a heteronuclear NMR study.
Biochemistry. 1994 Feb 8;33(5):1063-72
Authors: Alexandrescu AT, Abeygunawardana C, Shortle D
A partially folded form of staphylococcal nuclease has been obtained by deleting residues 4-12 and 141-149 of the 149-residue wild-type protein. Sequence-specific NMR resonance assignments have been obtained...
Structure and dynamics of the acid-denatured molten globule state of alpha-lactalbumi
Linear Mode
