Purification and characterization of 2S albumin from Nelumbo nucifera.

about

Purification and characterization of 2S albumin from Nelumbo nucifera.

Item

http://www.wikidata.org/entity/Q39929042

description

2016 nî lūn-bûn

@nan

2016年の論文

@ja

2016年論文

@yue

2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

@zh-mo

2016年論文

@zh-tw

2016年论文

@wuu

2016年论文

@zh

2016年论文

@zh-cn

name

Purification and characterization of 2S albumin from Nelumbo nucifera.

@en

Purification and characterization of 2S albumin from Nelumbo nucifera.

@nl

type

Item

label

Purification and characterization of 2S albumin from Nelumbo nucifera.

@en

Purification and characterization of 2S albumin from Nelumbo nucifera.

@nl

prefLabel

Purification and characterization of 2S albumin from Nelumbo nucifera.

@en

Purification and characterization of 2S albumin from Nelumbo nucifera.

@nl

P1476

Purification and characterization of 2S albumin from Nelumbo nucifera.

@en

P2093

Hidayatullah Khan

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

Mushtaq Ahmed

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

Sanaullah Khan

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

Syed Abid Ali

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

Tayyaba Yasmin

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

P2860

2S Albumin Storage Proteins: What Makes them Food Allergens?

Seed storage proteins: structures and biosynthesis

Refined solution structure of a liganded type 2 wheat nonspecific lipid transfer protein

Solution structure of RicC3, a 2S albumin storage protein from Ricinus communis

Solution Structure, Copper Binding and Backbone Dynamics of Recombinant Ber e 1–The Major Allergen from Brazil Nut

High-resolution crystal structure of the non-specific lipid-transfer protein from maize seedlings

Crystal structure of hydrophobic protein from soybean; a member of a new cysteine-rich family

1H NMR assignment and global fold of napin BnIb, a representative 2S albumin seed protein

Barley lipid-transfer protein complexed with palmitoyl CoA: the structure reveals a hydrophobic binding site that can expand to fit both large and small lipid-like ligands

Tertiary and quaternary structures of 0.19 alpha-amylase inhibitor from wheat kernel determined by X-ray analysis at 2.06 A resolution

P304

1-6

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

P31

scholarly article

P356

10.1080/09168451.2016.1158627

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

P577

2016-03-11T00:00:00Z

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

P698

26967322

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