Solution structure of the antimicrobial peptide gaegurin 4 by H and 15N nuclear magnetic resonance spectroscopy. - Wikidata - awgldk - TriplyDB

Solution structure of the antimicrobial peptide gaegurin 4 by H and 15N nuclear magnetic resonance spectroscopy.

Solution structure of the antimicrobial peptide gaegurin 4 by H and 15N nuclear magnetic resonance spectroscopy.

http://www.wikidata.org/entity/Q30593776

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On the role of NMR spectroscopy for characterization of antimicrobial peptides Solution structure and membrane-binding property of the N-terminal tail domain of human annexin I.Mechanisms of selective antimicrobial activity of gaegurin 4.Role of proline, cysteine and a disulphide bridge in the structure and activity of the anti-microbial peptide gaegurin 5.Structural study of novel antimicrobial peptides, nigrocins, isolated from Rana nigromaculata.Effects of salt and nickel ion on the conformational stability of Bacillus pasteurii UreE.Effects of a tryptophanyl substitution on the structure and antimicrobial activity of C-terminally truncated gaegurin 4.Systematic peptide engineering and structural characterization to search for the shortest antimicrobial peptide analogue of gaegurin 5.

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P2860

Solution structure of the antimicrobial peptide gaegurin 4 by H and 15N nuclear magnetic resonance spectroscopy.

http://www.wikidata.org/entity/Q30593776

description

2000 nî lūn-bûn

@nan

2000 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2000 թվականի մայիսին հրատարակված գիտական հոդված

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2000年の論文

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2000年論文

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2000年論文

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2000年論文

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2000年論文

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2000年論文

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2000年论文

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Solution structure of the anti ...... gnetic resonance spectroscopy.

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B J Lee

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B Lee

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J W Park

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S H Park

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Y K Kim

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Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor

A simple method for displaying the hydropathic character of a protein

Two-dimensional 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an alpha-helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution

fd coat protein structure in membrane environments: structural dynamics of the loop between the hydrophobic trans-membrane helix and the amphipathic in-plane helix

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NMRPipe: a multidimensional spectral processing system based on UNIX pipes

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fd coat protein structure in membrane environments.

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Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. Myohemerythrin.

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