Analyses of the stability and function of three surface mutants (R82C, K69H, and L32R) of the gene V protein from Ff phage by X-ray crystallography.

about

Importance of surrounding residues for protein stability of partially buried mutations.

P2860

Q52070827-BB1511C7-960C-4EF5-A3D1-C580363CA63A

P2860

Analyses of the stability and function of three surface mutants (R82C, K69H, and L32R) of the gene V protein from Ff phage by X-ray crystallography.

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http://www.wikidata.org/entity/Q36282278

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1997 nî lūn-bûn

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1997年の論文

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1997年学术文章

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1997年学术文章

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1997年学术文章

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1997年学术文章

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1997年学术文章

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1997年學術文章

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1997年學術文章

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1997年學術文章

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name

Analyses of the stability and ...... hage by X-ray crystallography.

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Analyses of the stability and ...... hage by X-ray crystallography.

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type

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Analyses of the stability and ...... hage by X-ray crystallography.

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Analyses of the stability and ...... hage by X-ray crystallography.

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prefLabel

Analyses of the stability and ...... hage by X-ray crystallography.

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Analyses of the stability and ...... hage by X-ray crystallography.

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P1476

Analyses of the stability and ...... hage by X-ray crystallography.

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P2093

A H Wang

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

H Zhang

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

S Su

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

T C Terwilliger

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

Y G Gao

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

P2860

Solution structure of the single-stranded DNA binding protein of the filamentous Pseudomonas phage Pf3: similarity to other proteins binding to single-stranded nucleic acids

Crystal structures of Y41H and Y41F mutants of gene V protein from Ff phage suggest possible protein-protein interactions in the GVP-ssDNA complex

Structure of the gene V protein of bacteriophage f1 determined by multiwavelength x-ray diffraction on the selenomethionyl protein

Context dependence of mutational effects in a protein: the crystal structures of the V35I, I47V and V35I/I47V gene V protein core mutants

Potential use of additivity of mutational effects in simplifying protein engineering

The solution structure of the Tyr41-->His mutant of the single-stranded DNA binding protein encoded by gene V of the filamentous bacteriophage M13.

Three-dimensional structure of complexes of single-stranded DNA-binding proteins with DNA. IKe and fd gene 5 proteins form left-handed helices with single-stranded DNA.

Neutron scattering data on reconstituted complexes of fd deoxyribonucleic acid and gene 5 protein show that the deoxyribonucleic acid is near the center.

Exploring the DNA binding domain of gene V protein encoded by bacteriophage M13 with the aid of spin-labeled oligonucleotides in combination with 1H-NMR.

13C NMR of methylated lysines of fd gene 5 protein: evidence for a conformational change involving lysine 24 upon binding of a negatively charged lanthanide chelate.

P304

771-780

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P31

scholarly article

P356

10.1002/PRO.5560060403

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

P478

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

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1997-04-01T00:00:00Z

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14118198

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P698

9098886

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P921

X-ray crystallography

P932

2144760

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

Analyses of the stability and function of three surface mutants (R82C, K69H, and L32R) of the gene V protein from Ff phage by X-ray crystallography.

about

P2860

P2860

Analyses of the stability and function of three surface mutants (R82C, K69H, and L32R) of the gene V protein from Ff phage by X-ray crystallography.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P5875

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P577

P5875

P698

P921

P932