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The program XEASY for computer-supported NMR spectral analysis of biological macromolecules (Q27860993)

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scientific article (publication date: July 1995)

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English	The program XEASY for computer-supported NMR spectral analysis of biological macromolecules	scientific article (publication date: July 1995)

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scholarly article

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The program XEASY for computer-supported NMR spectral analysis of biological macromolecules (English)

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5

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Christian Bartels

object named as

C Bartels

1

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Martin Billeter

3

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M Billeter

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author name string

T H Xia

2

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P Güntert

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publication date

July 1995

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language of work or name

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Journal of Biomolecular NMR

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6

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1

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1-10

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Protein secondary structure determination by NMR. Application with recombinant human cyclophilin.

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The nuclear-magnetic-resonance solution structure of the mutant alpha-amylase inhibitor [R19L] Tendamistat and comparison with wild-type Tendamistat

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https://pubmed.ncbi.nlm.nih.gov/22911575

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A computer-based protocol for semiautomated assignments and 3D structure determination of proteins

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https://pubmed.ncbi.nlm.nih.gov/22911575

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A spectral correlation function for efficient sequential NMR assignments of uniformly (15)N-labeled proteins

1 reference

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Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance

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Assignment of NMR spectra of proteins using triple-resonance two-dimensional experiments

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Efficient analysis of protein 2D NMR spectra using the software packageEASY

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Sequential assignment of 2D-NMR spectra of proteins using genetic algorithms

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A novel approach for sequential assignment of 1H, 13C, and 15N spectra of proteins: heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin

1 reference

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Structure determination of the Antp(C39 → S) homeodomain from nuclear magnetic resonance data in solution using a novel strategy for the structure calculation with the programs DIANA, CALIBA, HABAS and GLOMSA

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Application of neural networks to automated assignment of NMR spectra of proteins

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The nuclear magnetic resonance solution structure of the mixed disulfide between Escherichia coli glutaredoxin(C14S) and glutathione.

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NMR structure determination of the Escherichia coli DnaJ molecular chaperone: secondary structure and backbone fold of the N-terminal region (residues 2-108) containing the highly conserved J domain.

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Complete resonance assignment for the polypeptide backbone of interleukin 1.beta. using three-dimensional heteronuclear NMR spectroscopy

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Computer aided evaluation of two-dimensional NMR spectra of proteins

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3D 13C-15N-heteronuclear two-spin coherence spectroscopy for polypeptide backbone assignments in 13C-15N-double-labeled proteins.

1 reference

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Determination of the NMR solution structure of the cyclophilin A-cyclosporin A complex

1 reference

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Reduced dimensionality in triple-resonance NMR experiments

1 reference

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Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR

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Methodological advances in protein NMR

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Computer-assisted assignment of 2D 1H NMR spectra of proteins: basic algorithms and application to phoratoxin B.

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Processing of multi-dimensional NMR data with the new software PROSA

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Computer-Assisted Assignment of Homonuclear 3D NMR Spectra of Proteins. Application to Pike Parvalbumin III

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Computer-aided sequential assignment of protein 1H NMR spectra

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