Folding and stability of sweet protein single-chain monellin. An insight to protein engineering. (Q43715883)

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10 November 2019

title

Folding and stability of sweet protein single-chain monellin. An insight to protein engineering (English)

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10 November 2019

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2

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10 November 2019

author name string

Sung YH

1

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10 November 2019

Cheong C

3

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10 November 2019

Kim JH

4

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10 November 2019

Cho JM

5

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10 November 2019

Kim YR

6

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10 November 2019

Lee W

7

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language of work or name

English

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publication date

21 August 2001

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Journal of Biological Chemistry

10 November 2019

published in

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10 November 2019

volume

276

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10 November 2019

issue

47

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10 November 2019

page(s)

44229-44238

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Protein Folding: A Perspective from Theory and Experiment.

10 November 2019

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Electrophysiological study of the gustatory effects of the sweet proteins monellin and thaumatin in monkey, guinea pig and rat.

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Crystal structure of the intensely sweet protein monellin

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Structural characterization of monellin in the alcohol-denatured state by NMR: evidence for beta-sheet to alpha-helix conversion

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Sweet-tasting protein monellin is related to the cystatin family of thiol proteinase inhibitors.

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Redesigning a sweet protein: increased stability and renaturability

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Solution structure of a sweet protein single-chain monellin determined by nuclear magnetic resonance and dynamical simulated annealing calculations

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Solution structure, backbone dynamics, and stability of a double mutant single-chain monellin. structural origin of sweetness

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Identifiers

DOI

10.1074/JBC.M104239200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11517219%20AND%20SRC:MED&resulttype=core&format=json

10 November 2019

1 reference