(Q57889932)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9253412%20AND%20SRC:MED&resulttype=core&format=json

5 November 2019

title

A residue-specific NMR view of the non-cooperative unfolding of a molten globule (English)

1 reference

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5 November 2019

0 references

4

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5 November 2019

author name string

B A Schulman

series ordinal

1

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9253412%20AND%20SRC:MED&resulttype=core&format=json

5 November 2019

P S Kim

series ordinal

2

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9253412%20AND%20SRC:MED&resulttype=core&format=json

5 November 2019

C M Dobson

series ordinal

3

1 reference

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5 November 2019

publication date

1 August 1997

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9253412%20AND%20SRC:MED&resulttype=core&format=json

Nature structural biology

5 November 2019

published in

1 reference

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5 November 2019

volume

4

1 reference

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5 November 2019

issue

8

1 reference

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5 November 2019

page(s)

630-634

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Is Apomyoglobin a Molten Globule? Structural Characterization by NMR

5 November 2019

cites work

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Toward a Description of the Conformations of Denatured States of Proteins. Comparison of a Random Coil Model with NMR Measurements

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Different subdomains are most protected from hydrogen exchange in the molten globule and native states of human alpha-lactalbumin

21 January 2018

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Stable submolecular folding units in a non-compact form of cytochrome c

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Determination and analysis of urea and guanidine hydrochloride denaturation curves

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The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure.

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Protein folding. Solid evidence for molten globules

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A protein dissection study of a molten globule

31 March 2020

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Bipartite structure of the alpha-lactalbumin molten globule

31 March 2020

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Probing the stability of a partly folded apomyoglobin intermediate by site-directed mutagenesis

31 March 2020

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Molten globular characteristics of the native state of apomyoglobin

31 March 2020

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Packing interactions in the apomyglobin folding intermediate

31 March 2020

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The molten globule state of alpha-lactalbumin.

31 March 2020

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Characterization of a partly folded protein by NMR methods: studies on the molten globule state of guinea pig alpha-lactalbumin

31 March 2020

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The equilibrium folding pathway of staphylococcal nuclease: identification of the most stable chain-chain interactions by NMR and CD spectroscopy

31 March 2020

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Initial studies of the equilibrium folding pathway of staphylococcal nuclease

31 March 2020

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Relationship between nuclear magnetic resonance chemical shift and protein secondary structure

31 March 2020

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Local structural preferences in the alpha-lactalbumin molten globule.

31 March 2020

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Structure and dynamics of the acid-denatured molten globule state of alpha-lactalbumin: a two-dimensional NMR study

31 March 2020

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Structure and stability of the molten globule state of guinea-pig alpha-lactalbumin: a hydrogen exchange study

31 March 2020

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Proline scanning mutagenesis of a molten globule reveals non-cooperative formation of a protein's overall topology.

31 March 2020

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Structural basis of the stability of a lysozyme molten globule

31 March 2020

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Probing the partly folded states of proteins by limited proteolysis

31 March 2020

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All-or-none solvent-induced transitions between native, molten globule and unfolded states in globular proteins

31 March 2020

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Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin

31 March 2020

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Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway

31 March 2020

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Refolding and unfolding kinetics of the equilibrium folding intermediate of apomyoglobin

31 March 2020

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Unfolding of the molten globule state of alpha-lactalbumin studied by 1H NMR

31 March 2020

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Calorimetric determination of the energetics of the molten globule intermediate in protein folding: apo-alpha-lactalbumin

31 March 2020

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Absence of the thermal transition in apo-alpha-lactalbumin in the molten globule state. A study by differential scanning microcalorimetry

31 March 2020

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Following protein folding in real time using NMR spectroscopy

31 March 2020

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Rapid formation of a molten globule intermediate in refolding of alpha-lactalbumin

31 March 2020

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Overcoming the overlap problem in the assignment of 1H NMR spectra of larger proteins by use of three-dimensional heteronuclear 1H-15N Hartmann-Hahn-multiple quantum coherence and nuclear Overhauser-multiple quantum coherence spectroscopy: applicati

31 March 2020

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Complete resonance assignment for the polypeptide backbone of interleukin 1.beta. using three-dimensional heteronuclear NMR spectroscopy

31 March 2020

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Crystal structure of human α-lactalbumin at 1·7 Å resolution

31 March 2020

1 reference

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31 March 2020

Identifiers

DOI

10.1038/NSB0897-630

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9253412%20AND%20SRC:MED&resulttype=core&format=json

5 November 2019

1 reference