Influence of pH on the structure and stability of the sweet protein MNEI.

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Getting value from the waste: recombinant production of a sweet protein by Lactococcus lactis grown on cheese whey

P2860

Q58777951-14C73FAD-F507-4464-B23A-B220F09BC301

P2860

Influence of pH on the structure and stability of the sweet protein MNEI.

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http://www.wikidata.org/entity/Q48282757

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2016 nî lūn-bûn

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2016年の論文

@ja

2016年学术文章

@wuu

2016年学术文章

@zh

2016年学术文章

@zh-cn

2016年学术文章

@zh-hans

2016年学术文章

@zh-my

2016年学术文章

@zh-sg

2016年學術文章

@yue

2016年學術文章

@zh-hant

name

Influence of pH on the structure and stability of the sweet protein MNEI.

@en

Influence of pH on the structure and stability of the sweet protein MNEI.

@nl

type

Item

label

Influence of pH on the structure and stability of the sweet protein MNEI.

@en

Influence of pH on the structure and stability of the sweet protein MNEI.

@nl

prefLabel

Influence of pH on the structure and stability of the sweet protein MNEI.

@en

Influence of pH on the structure and stability of the sweet protein MNEI.

@nl

P1476

Influence of pH on the structure and stability of the sweet protein MNEI.

@en

P2093

Christian Richter

http://www.w3.org/2001/XMLSchema#string

Delia Picone

http://www.w3.org/2001/XMLSchema#string

Michele Fortunato Rega

http://www.w3.org/2001/XMLSchema#string

P2860

Solution structure of a sweet protein: NMR study of MNEI, a single chain monellin

The pKa Values of Acidic and Basic Residues Buried at the Same Internal Location in a Protein Are Governed by Different Factors

NMR Studies on Structure and Dynamics of the Monomeric Derivative of BS-RNase: New Insights for 3D Domain Swapping

Two crystal structures of a potently sweet protein. Natural monellin at 2.75 A resolution and single-chain monellin at 1.7 A resolution

Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation

Probing the surface of a sweet protein: NMR study of MNEI with a paramagnetic probe

Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease

Primary structure effects on peptide group hydrogen exchange

An evaluation of the use of hydrogen exchange at equilibrium to probe intermediates on the protein folding pathway.

Toward the understanding of MNEI sweetness from hydration map surfaces

P304

3681-3689

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P31

scholarly article

P356

10.1002/1873-3468.12437

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P407

English

P433

http://www.w3.org/2001/XMLSchema#string

P478

590

http://www.w3.org/2001/XMLSchema#string

P50

Serena Leone

Roberta Spadaccini

P577

2016-09-29T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

27685084

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Influence of pH on the structure and stability of the sweet protein MNEI.

about

P2860

P2860

Influence of pH on the structure and stability of the sweet protein MNEI.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698