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Literature DB >> 9675166

Neutron off-plane scattering of aligned membranes. I. Method Of measurement.

L Yang¹, T A Harroun, W T Heller, T M Weiss, H W Huang.

Abstract

We describe a method of measuring neutron scattering of aligned membranes with the momentum transfer oriented parallel or partly perpendicular to the plane of the membranes. The method obtains the complete information for the structures within fluid membranes obtainable by scattering. Data from alamethicin- and magainin-induced pores are presented. Although the in-plane scattering curves of these two peptides are similar to each other, their off-plane scattering patterns are strikingly distinct. Magainin pores exhibit intermembrane correlations.

Entities: Chemical

Mesh：

Substances：

Year: 1998 PMID： 9675166 PMCID： PMC1299739 DOI： 10.1016/S0006-3495(98)77554-X

Source DB: PubMed Journal: Biophys J ISSN： 0006-3495 Impact factor: 4.033

5 in total

1. Membrane pores induced by magainin.

Authors: S J Ludtke; K He; W T Heller; T A Harroun; L Yang; H W Huang
Journal: Biochemistry Date: 1996-10-29 Impact factor: 3.162

2. Uniformly oriented gramicidin channels embedded in thick monodomain lecithin multilayers.

Authors: H W Huang; G A Olah
Journal: Biophys J Date: 1987-06 Impact factor: 4.033

3. Membrane thinning caused by magainin 2.

Authors: S Ludtke; K He; H Huang
Journal: Biochemistry Date: 1995-12-26 Impact factor: 3.162

4. Neutron scattering in the plane of membranes: structure of alamethicin pores.

Authors: K He; S J Ludtke; D L Worcester; H W Huang
Journal: Biophys J Date: 1996-06 Impact factor: 4.033

5. Method of oriented circular dichroism.

Authors: Y Wu; H W Huang; G A Olah
Journal: Biophys J Date: 1990-04 Impact factor: 3.699

5 in total

19 in total

1. Supramolecular structures of peptide assemblies in membranes by neutron off-plane scattering: method of analysis.

Authors: L Yang; T M Weiss; T A Harroun; W T Heller; H W Huang
Journal: Biophys J Date: 1999-11 Impact factor: 4.033

2. Crystallization of antimicrobial pores in membranes: magainin and protegrin.

Authors: L Yang; T M Weiss; R I Lehrer; H W Huang
Journal: Biophys J Date: 2000-10 Impact factor: 4.033

3. Barrel-stave model or toroidal model? A case study on melittin pores.

Authors: L Yang; T A Harroun; T M Weiss; L Ding; H W Huang
Journal: Biophys J Date: 2001-09 Impact factor: 4.033

4. A rhombohedral phase of lipid containing a membrane fusion intermediate structure.

Authors: Lin Yang; Huey W Huang
Journal: Biophys J Date: 2003-03 Impact factor: 4.033

5. The CpxR/CpxA two-component system up-regulates two Tat-dependent peptidoglycan amidases to confer bacterial resistance to antimicrobial peptide.

Authors: Natasha Weatherspoon-Griffin; Guang Zhao; Wei Kong; Ying Kong; Helene Andrews-Polymenis; Michael McClelland; Yixin Shi
Journal: J Biol Chem Date: 2010-12-13 Impact factor: 5.157

Neutron off-plane scattering of aligned membranes. I. Method Of measurement.

1. Membrane pores induced by magainin.

2. Uniformly oriented gramicidin channels embedded in thick monodomain lecithin multilayers.

3. Membrane thinning caused by magainin 2.

4. Neutron scattering in the plane of membranes: structure of alamethicin pores.

5. Method of oriented circular dichroism.

1. Supramolecular structures of peptide assemblies in membranes by neutron off-plane scattering: method of analysis.

2. Crystallization of antimicrobial pores in membranes: magainin and protegrin.

3. Barrel-stave model or toroidal model? A case study on melittin pores.

4. A rhombohedral phase of lipid containing a membrane fusion intermediate structure.

5. The CpxR/CpxA two-component system up-regulates two Tat-dependent peptidoglycan amidases to confer bacterial resistance to antimicrobial peptide.

6. Structure of the alamethicin pore reconstructed by x-ray diffraction analysis.

7. Structure of transmembrane pore induced by Bax-derived peptide: evidence for lipidic pores.

8. Process of inducing pores in membranes by melittin.

9. Comparative Study of the Condensing Effects of Ergosterol and Cholesterol.

10. De novo design of potent antimicrobial peptides.