NMR Structural Studies of Antimicrobial Peptides: LPcin Analogs.

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Membrane Active Antimicrobial Peptides: Translating Mechanistic Insights to Design.Mode of Action of a Designed Antimicrobial Peptide: High Potency against Cryptococcus neoformans.Membrane Active Peptides and Their Biophysical Characterization

P2860

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P2860

NMR Structural Studies of Antimicrobial Peptides: LPcin Analogs.

Item

http://www.wikidata.org/entity/Q40083533

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2016 nî lūn-bûn

@nan

2016 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2016年の論文

@ja

2016年論文

@yue

2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

@zh-mo

2016年論文

@zh-tw

2016年论文

@wuu

2016年论文

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name

NMR Structural Studies of Antimicrobial Peptides: LPcin Analogs.

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type

Item

label

NMR Structural Studies of Antimicrobial Peptides: LPcin Analogs.

@en

prefLabel

NMR Structural Studies of Antimicrobial Peptides: LPcin Analogs.

@en

P1476

NMR Structural Studies of Antimicrobial Peptides: LPcin Analogs.

@en

P2093

Ji-Ho Jeong

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

Ji-Sun Kim

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

Sung-Sub Choi

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

Yongae Kim

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

P2860

Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy

Three-dimensional structure of the channel-forming trans-membrane domain of virus protein "u" (Vpu) from HIV-1

Conformational changes induced by a single amino acid substitution in thetrans-membrane domain of Vpu: Implications for HIV-1 susceptibility to channel blocking drugs

Structure Determination of a Membrane Protein in Proteoliposomes

NMRPipe: a multidimensional spectral processing system based on UNIX pipes

Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium

Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels

NMR structure of the integral membrane protein OmpX.

Biophysical approaches to membrane protein structure determination.

Structural characterization of folded and unfolded states of an SH3 domain in equilibrium in aqueous buffer.

P304

423-430

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P31

scholarly article

P356

10.1016/J.BPJ.2015.12.006

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P407

English

P433

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

P478

110

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P577

2016-01-01T00:00:00Z

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P698

26789765

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P932

4724650

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NMR Structural Studies of Antimicrobial Peptides: LPcin Analogs.

about

P2860

P2860

NMR Structural Studies of Antimicrobial Peptides: LPcin Analogs.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698

P932