Structural Feature of Lipid Scrambling Model Transmembrane Peptides: Same-Side Positioning of Hydrophilic Residues and Their Deeper Position

This article builds a framework for a relational approach to segregation that emphasizes structures of interactions, transactions, and ties between and within social categories. Rather than explaining segregation with dominants imposing formal rules or homophilic people sorting themselves, I highlight segregation’s emergence amid dueling control efforts among actors with malleable categorical identities. And rather than assuming segregation necessarily fuels cycles of inequality or persecution, I identify nuanced advantages and disadvantages for different actors in social conflict. I also explore an underappreciated role of institutions in segregation: They guide relations across different domains of activity that may have different degrees of segregation. An overarching theme is that segregation is not a specific thing with regular causes and effects but an inherently contradictory structural feature of relations that evolves as actors struggle for control.

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STRUCTURAL FEATURE OF ANTIBIOTIC A-396-I

The Journal of Antibiotics ◽

10.7164/antibiotics.23.569 ◽

1970 ◽

Vol 23 (11) ◽

pp. 569-571 ◽

Cited By ~ 10

Author(s):

JUN''ICHI SHOJI ◽

YUZO NAKAGAWA

Keyword(s):

Structural Feature

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The structural feature surrounding glycated lysine residues in human hemoglobin

Biomedical Research ◽

10.2220/biomedres.32.217 ◽

2011 ◽

Vol 32 (3) ◽

pp. 217-223 ◽

Cited By ~ 11

Author(s):

Shigenori Ito ◽

Takashi Nakahari ◽

Daisuke Yamamoto

Keyword(s):

Structural Feature ◽

Human Hemoglobin ◽

Lysine Residues

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Studies of transmembrane peptides by pulse dipolar spectroscopy with semi-rigid TOPP spin labels

European Biophysics Journal ◽

10.1007/s00249-021-01508-6 ◽

2021 ◽

Author(s):

Igor Tkach ◽

Ulf Diederichsen ◽

Marina Bennati

Keyword(s):

Molecular Level ◽

Dipolar Interaction ◽

Spin Labels ◽

Paramagnetic Centers ◽

Structural Adaptation ◽

Paramagnetic Resonance ◽

Transmembrane Peptides ◽

Distance Distributions ◽

Lipid Environment ◽

Electron Paramagnetic

AbstractElectron paramagnetic resonance (EPR)-based pulsed dipolar spectroscopy measures the dipolar interaction between paramagnetic centers that are separated by distances in the range of about 1.5–10 nm. Its application to transmembrane (TM) peptides in combination with modern spin labelling techniques provides a valuable tool to study peptide-to-lipid interactions at a molecular level, which permits access to key parameters characterizing the structural adaptation of model peptides incorporated in natural membranes. In this mini-review, we summarize our approach for distance and orientation measurements in lipid environment using novel semi-rigid TOPP [4-(3,3,5,5-tetramethyl-2,6-dioxo-4-oxylpiperazin-1-yl)-L-phenylglycine] labels specifically designed for incorporation in TM peptides. TOPP labels can report single peak distance distributions with sub-angstrom resolution, thus offering new capabilities for a variety of TM peptide investigations, such as monitoring of various helix conformations or measuring of tilt angles in membranes. Graphical Abstract

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Screening for novel cell adhesive regions in bovine Achilles tendon collagen peptides

Biochemistry and Cell Biology ◽

10.1139/bcb-2013-0026 ◽

2014 ◽

Vol 92 (1) ◽

pp. 9-22 ◽

Cited By ~ 6

Author(s):

Pradipta Banerjee ◽

Alka Mehta ◽

C. Shanthi

Keyword(s):

Cell Adhesion ◽

Docking Studies ◽

Exchange Chromatography ◽

Adhesion Assay ◽

Structural Protein ◽

Cell Adherence ◽

Collagen Peptides ◽

Adhesion Ability ◽

A Cell ◽

Hydrophilic Residues

Collagen, a major structural protein of the ECM, is known for its high cell adherence capacity. This study was conducted to identify regions in collagen that harbour such bioactivity. Collagen from tendon was hydrolysed and the peptides fractionated using ion-exchange chromatography (IEC). Isolated peptide fractions were coated onto disposable dishes and screened for cell adherence and proliferative abilities. Active IEC fractions were further purified by chromatography, and two peptides, C2 and E1 with cell adhesion ability, were isolated. A cell adhesion assay done with different amounts of C2 coated onto disposable dishes revealed the maximum adhesion to be 94.6%, compared with 80% for collagen coated dishes and an optimum peptide coating density of 0.507 nmoles per cm2 area of the dish. Growth of cells on C2, collagen, and E1 revealed a similar pattern and a reduction in the doubling time compared with cells grown on uncoated dishes. C2 had a mass of 2.046 kDa with 22 residues, and sequence analysis revealed a higher percentage occurrence of hydrophilic residues compared with other regions in collagen. Docking studies revealed GDDGEA in C2 as the probable site of interaction with integrins α2β1 and α1β1, and stability studies proved C2 to be mostly protease-resistant.

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