(Q36633764)

15 August 2017

title

Structure of Alamethicin in solution. One- and two-dimensional 1H nuclear magnetic resonance studies at 500 MHz. (English)

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ORCID Public Data File 2021

15 August 2017

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author name string

Banerjee U

1

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15 August 2017

Tsui FP

2

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15 August 2017

Balasubramanian TN

3

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15 August 2017

Marshall GR

4

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15 August 2017

Chan SI

5

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15 August 2017

language of work or name

English

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publication date

1 April 1983

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Journal of Molecular Biology

15 August 2017

published in

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15 August 2017

volume

165

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15 August 2017

issue

4

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15 August 2017

page(s)

757-775

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A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules

15 August 2017

cites work

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The nature of the voltage-dependent conductance induced by alamethicin in black lipid membranes

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Kinetics and stability of alamethicin conducting channels in lipid bilayers.

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Voltage-dependent lipid flip-flop induced by alamethicin

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Nuclear magnetic resonance studies of the polypeptide alamethicin and its interaction with phospholipids.

7 January 2021

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[The hemolytic properties of the membrane modifying peptide antibiotics alamethicin, suzukacillin and trichotoxin (author's transl)]

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Chemical nature and sequence of alamethicin

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Alamethicin and synthetic peptide fragments as uncouplers of mitochondrial oxidative phosphorylation. Effect of chain length and charge

7 January 2021

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The aggregation of alamethicin

7 January 2021

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The conformation of alamethicin

7 January 2021

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Conformations of synthetic alamethicin fragments. Evidence for 310 helical folding from 270-MHz hydrogen-1 nuclear magnetic resonance and circular dichroism studies

7 January 2021

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Infrared studies on the conformation of synthetic alamethicin fragments and model peptides containing alpha-aminoisobutyric acid

7 January 2021

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Systematic application of two-dimensional 1H nuclear-magnetic-resonance techniques for studies of proteins. 2. Combined use of correlated spectroscopy and nuclear Overhauser spectroscopy for sequential assignments of backbone resonances and elucidat

7 January 2021

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Sequential resonance assignments as a basis for determination of spatial protein structures by high resolution proton nuclear magnetic resonance

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Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra. Basic pancreatic trypsin inhibitor

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inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1016/S0022-2836(83)80279-4

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15 August 2017

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