Beta7E-beta132K salt bridge and sickle haemoglobin stability and conformation.

about

Liganded hemoglobin structural perturbations by the allosteric effector L35.

P2860

Q34189425-7E4539FB-BE04-4BB5-AB38-04EF8AE0B149

P2860

Beta7E-beta132K salt bridge and sickle haemoglobin stability and conformation.

Item

http://www.wikidata.org/entity/Q44503976

description

2003 nî lūn-bûn

@nan

2003年の論文

@ja

2003年学术文章

@wuu

2003年学术文章

@zh

2003年学术文章

@zh-cn

2003年学术文章

@zh-hans

2003年学术文章

@zh-my

2003年学术文章

@zh-sg

2003年學術文章

@yue

2003年學術文章

@zh-hant

name

Beta7E-beta132K salt bridge and sickle haemoglobin stability and conformation.

@en

Beta7E-beta132K salt bridge and sickle haemoglobin stability and conformation.

@nl

type

Item

label

Beta7E-beta132K salt bridge and sickle haemoglobin stability and conformation.

@en

Beta7E-beta132K salt bridge and sickle haemoglobin stability and conformation.

@nl

prefLabel

Beta7E-beta132K salt bridge and sickle haemoglobin stability and conformation.

@en

Beta7E-beta132K salt bridge and sickle haemoglobin stability and conformation.

@nl

P1476

Beta7E-beta132K salt bridge and sickle haemoglobin stability and conformation.

@en

P2093

Christophe Fablet

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

Josée Pagnier

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

Michael C Marden

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

Qiuying Chen

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

Rhoda Elison Hirsch

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

Ronald L Nagel

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

Véronique Baudin-Creuza

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

P2860

The high resolution crystal structure of deoxyhemoglobin S

Pathogenesis of hemolytic anemia in homozygous hemoglobin C disease

Surface activity of hemoglobin S and other human hemoglobin variants.

Effects of amino acid substitutions at beta 131 on the structure and properties of hemoglobin: evidence for communication between alpha 1 beta 1- and alpha 1 beta 2-subunit interfaces.

Conformational changes in hemoglobin S (betaE6V) imposed by mutation of the beta Glu7-beta Lys132 salt bridge and detected by UV resonance Raman spectroscopy.

Global allostery model of hemoglobin. Modulation of O(2) affinity, cooperativity, and Bohr effect by heterotropic allosteric effectors.

P304

317-325

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

P31

scholarly article

P356

10.1046/J.1365-2141.2003.04432.X

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

P407

English

P433

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

P478

122

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

P577

2003-07-01T00:00:00Z

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

P5875

10673652

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

P698

12846903

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

Beta7E-beta132K salt bridge and sickle haemoglobin stability and conformation.

about

P2860

P2860

Beta7E-beta132K salt bridge and sickle haemoglobin stability and conformation.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P5875

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P5875

P698