Quaternary structure and function in phage lambda repressor: 1H-NMR studies of genetically altered proteins.

about

Papain does not cleave operator-bound lambda repressor: structural characterization of the carboxy terminal domain and the hinge.

P2860

Q43540087-5B6B3966-755B-4DFC-A032-DC47B6C01F09

P2860

Quaternary structure and function in phage lambda repressor: 1H-NMR studies of genetically altered proteins.

Item

http://www.wikidata.org/entity/Q43444658

description

1987 nî lūn-bûn

@nan

1987年の論文

@ja

1987年学术文章

@wuu

1987年学术文章

@zh

1987年学术文章

@zh-cn

1987年学术文章

@zh-hans

1987年学术文章

@zh-my

1987年学术文章

@zh-sg

1987年學術文章

@yue

1987年學術文章

@zh-hant

name

Quaternary structure and funct ...... genetically altered proteins.

@en

Quaternary structure and funct ...... genetically altered proteins.

@nl

type

Item

label

Quaternary structure and funct ...... genetically altered proteins.

@en

Quaternary structure and funct ...... genetically altered proteins.

@nl

prefLabel

Quaternary structure and funct ...... genetically altered proteins.

@en

Quaternary structure and funct ...... genetically altered proteins.

@nl

P1476

Quaternary structure and funct ...... genetically altered proteins.

@en

P2093

Karplus M

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

Sauer RT

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

Weiss MA

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

P2860

Comparisons of ring-current shifts calculated from the crystal structure of egg white lysozyme of hen with the proton nuclear magnetic resonance spectrum of lysozyme in solution.

Structure of the cro repressor from bacteriophage lambda and its interaction with DNA.

The operator-binding domain of lambda repressor: structure and DNA recognition.

The three-dimensional structure of trp repressor.

Recognition sequences of repressor and polymerase in the operators of bacteriophage lambda.

Cocrystals of the DNA-binding domain of phage 434 repressor and a synthetic phage 434 operator.

Possible ideal lac operator: Escherichia coli lac operator-like sequences from eukaryotic genomes lack the central G X C pair.

The lambda repressor contains two domains.

Secondary structure of the lac repressor DNA-binding domain by two-dimensional 1H nuclear magnetic resonance in solution.

Mutations in lambda repressor's amino-terminal domain: implications for protein stability and DNA binding.

P304

539-556

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

P31

scholarly article

P356

10.1080/07391102.1987.10506412

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

P433

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

P478

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

P577

1987-12-01T00:00:00Z

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

P698

2978735

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

Quaternary structure and function in phage lambda repressor: 1H-NMR studies of genetically altered proteins.

about

P2860

P2860

Quaternary structure and function in phage lambda repressor: 1H-NMR studies of genetically altered proteins.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P698