Interaction of urea with an unfolded protein. The DNA-binding domain of the 434-repressor (Q36708663)

15 August 2017

title

Interaction of urea with an unfolded protein. The DNA-binding domain of the 434-repressor (English)

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15 August 2017

4

Wüthrich K

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15 August 2017

Dötsch V

1

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15 August 2017

Wider G

series ordinal

2

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15 August 2017

Siegal G

series ordinal

3

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15 August 2017

language of work or name

English

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publication date

1 June 1995

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15 August 2017

number of pages

5

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based on heuristic

inferred from page(s)

published in

FEBS Letters

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15 August 2017

volume

366

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15 August 2017

issue

1

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15 August 2017

page(s)

6-10

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Water as ligand: preferential binding and exclusion of denaturants in protein unfolding

15 August 2017

cites work

1 reference

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A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range

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Kinetics and mechanism of the folding of cytochrome c

21 January 2018

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Equilibrium denaturation of recombinant human FK binding protein in urea

21 January 2018

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Aggregation and denaturation of apomyoglobin in aqueous urea solutions

21 January 2018

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21 January 2018

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1H, 15N and 13C NMR assignments of the 434 repressor fragments 1-63 and 44-63 unfolded in 7 M urea.

21 January 2018

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Determination of the three-dimensional structure of the Antennapedia homeodomain from Drosophila in solution by 1H nuclear magnetic resonance spectroscopy

21 January 2018

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Protein hydration studied with homonuclear 3D1H NMR experiments

21 January 2018

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A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules

21 January 2018

1 reference

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Determination of the nuclear magnetic resonance solution structure of the DNA-binding domain (residues 1 to 69) of the 434 repressor and comparison with the X-ray crystal structure

21 January 2018

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NMR spectroscopy of hydroxyl protons in aqueous solutions of peptides and proteins.

21 January 2018

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Steric exclusion is the principal source of the preferential hydration of proteins in the presence of polyethylene glycols

21 January 2018

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Urea denaturation of barnase: pH dependence and characterization of the unfolded state

21 January 2018

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NMR determination of residual structure in a urea-denatured protein, the 434-repressor

21 January 2018

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Protein hydration in aqueous solution

21 January 2018

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11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/0014-5793(95)00459-M

Protein interactions with urea and guanidinium chloride. A calorimetric study

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11 October 2022

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Expression of functionality of alpha-chymotrypsin. Effects of guanidine hydrochloride and urea in the onset of denaturation

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11 October 2022

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Identifiers

DOI

10.1016/0014-5793(95)00459-M

1 reference

release_d5z2zekdljc5xggnotwyiuhamq

15 August 2017

Fatcat ID

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Fatcat

https://api.fatcat.wiki/v0/release/d5z2zekdljc5xggnotwyiuhamq

mapped directly with Wikidata item

24 November 2022

based on heuristic

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