GENFOLD: a genetic algorithm for folding protein structures using NMR restraints.

Item

http://www.wikidata.org/entity/Q42123021

description

1998 nî lūn-bûn

@nan

1998年の論文

@ja

1998年論文

@yue

1998年論文

@zh-hant

1998年論文

@zh-hk

1998年論文

@zh-mo

1998年論文

@zh-tw

1998年论文

@wuu

1998年论文

@zh

1998年论文

@zh-cn

name

GENFOLD: a genetic algorithm for folding protein structures using NMR restraints.

@en

GENFOLD: a genetic algorithm for folding protein structures using NMR restraints.

@nl

type

Item

label

GENFOLD: a genetic algorithm for folding protein structures using NMR restraints.

@en

GENFOLD: a genetic algorithm for folding protein structures using NMR restraints.

@nl

prefLabel

GENFOLD: a genetic algorithm for folding protein structures using NMR restraints.

@en

GENFOLD: a genetic algorithm for folding protein structures using NMR restraints.

@nl

P1476

GENFOLD: a genetic algorithm for folding protein structures using NMR restraints.

@en

P2093

Bayley MJ

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

Jones G

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

Willett P

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

Williamson MP

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

P2860

Determination of a high-quality nuclear magnetic resonance solution structure of the bovine pancreatic trypsin inhibitor and comparison with three crystal structures

Solution conformation of proteinase inhibitor IIA from bull seminal plasma by 1H nuclear magnetic resonance and distance geometry

Solution structure of the granular starch binding domain of glucoamylase from Aspergillus niger by nuclear magnetic resonance spectroscopy

The Protein Data Bank: a computer-based archival file for macromolecular structures

Development and validation of a genetic algorithm for flexible docking

An evaluation of the combined use of nuclear magnetic resonance and distance geometry for the determination of protein conformations in solution

Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA

Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints.

Global fold determination from a small number of distance restraints.

An evolutionary approach to folding small alpha-helical proteins that uses sequence information and an empirical guiding fitness function.

P304

491-499

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

P31

scholarly article

P356

10.1002/PRO.5560070230

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

P433

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

P478

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

P577

1998-02-01T00:00:00Z

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

P5875

227632555

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

P698

9521126

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

P921

protein folding

P932

2143927

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