(Q47740710)

5 February 2018

title

Appropriateness of DSS and TSP as internal references for (1)H NMR studies of molten globule proteins in aqueous media. (English)

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5 February 2018

author name string

A Shimizu

series ordinal

1

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5 February 2018

M Ikeguchi

series ordinal

2

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5 February 2018

S Sugai

series ordinal

3

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5 February 2018

publication date

1 November 1994

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5 February 2018

Journal of Biomolecular NMR

published in

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5 February 2018

volume

4

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5 February 2018

page(s)

859-862

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5 February 2018

issue

6

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5 February 2018

https://scigraph.springernature.com/pub.10.1007/bf00398414

exact match

0 references

cites work

Partially folded conformation of the (30-51) intermediate in the disulphide folding pathway of bovine pancreatic trypsin inhibitor. 1H and 15N resonance assignments and determination of backbone dynamics from 15N relaxation measurements.

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12 December 2020

Dissecting the structure of a partially folded protein. Circular dichroism and nuclear magnetic resonance studies of peptides from ubiquitin

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12 December 2020

Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe

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12 December 2020

Characterization of a trifluoroethanol-induced partially folded state of alpha-lactalbumin

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12 December 2020

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

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12 December 2020

Molten-globule conformation of Arc repressor monomers determined by high-pressure 1H NMR spectroscopy.

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12 December 2020

A partially folded state of hen egg white lysozyme in trifluoroethanol: structural characterization and implications for protein folding

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12 December 2020

Structure and dynamics of a denatured 131-residue fragment of staphylococcal nuclease: a heteronuclear NMR study

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12 December 2020

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

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12 December 2020

Hydrophobic clustering in nonnative states of a protein: interpretation of chemical shifts in NMR spectra of denatured states of lysozyme

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12 December 2020

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

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12 December 2020

Acid-induced folding of proteins

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12 December 2020

Spectrofluorimetric assessment of the surface hydrophobicity of proteins

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12 December 2020

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

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12 December 2020

The evolution of lysozyme and alpha-lactalbumin

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12 December 2020

Structural characterization of the FK506 binding protein unfolded in urea and guanidine hydrochloride

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12 December 2020

Heteronuclear three-dimensional NMR spectroscopy of a partially denatured protein: the A-state of human ubiquitin.

1 reference

12 December 2020

Identifiers

DOI

10.1007/BF00398414

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5 February 2018

PubMed ID

22911388

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5 February 2018