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Monohybrid Crosses01:20

Monohybrid Crosses

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Cross-reactivity00:42

Cross-reactivity

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Trihybrid Crosses

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Some of Mendel’s crosses examined three pairs of contrasting characteristics. Such a cross is called a trihybrid cross. A trihybrid cross is a combination of three individual monohybrid crosses. For example, plant height (tall vs. short), seed shape (round vs. wrinkled), and seed color (yellow vs. green).
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In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
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Crossed Aldol Reactions: Overview01:04

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Chemo-enzymatic Synthesis of N-glycans for Array Development and HIV Antibody Profiling
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Published on: February 5, 2018

Amyloid and the Cross-Beta Architecture.

Kyle Morris1, Karen E Marshall1, Youssra Al-Hilaly1

  • 1School of Life Sciences, University of Sussex.

Journal of Visualized Experiments : Jove
|March 2, 2026
PubMed
Summary
This summary is machine-generated.

Amyloid fibrils, implicated in diseases like Alzheimer's, possess a repetitive structure. This study details methods to determine this architecture across various amyloid fibril sources.

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Last Updated: Jul 3, 2026

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Area of Science:

  • Structural biology
  • Biochemistry
  • Biophysics

Background:

  • Amyloid fibrils are misfolded protein assemblies with repetitive structures.
  • They are associated with diseases such as Alzheimer's and type 2 diabetes.
  • Functional roles in organisms include providing strength and scaffolding.

Purpose of the Study:

  • To describe methods for determining the underlying architecture of amyloid fibrils.
  • To highlight common features of amyloid fibrils from diverse sources.
  • To provide a framework for comparing experimental data with model structures.

Main Methods:

  • X-ray fiber diffraction was initially used to model amyloid structures.
  • Advanced diffraction analysis of oriented and semi-crystalline samples provides detailed architecture.
  • Methods cover sample preparation, data collection, and data analysis.

Main Results:

  • Detailed structural models of the generic cross-β structure have been developed.
  • Analysis reveals the organization of peptides into repetitive architectures.
  • Common features across pathogenic, functional, and synthetic amyloid fibrils are described.

Conclusions:

  • Understanding amyloid fibril architecture is crucial for studying protein misfolding diseases.
  • The described methods enable detailed structural characterization of diverse amyloid fibrils.
  • This work facilitates comparison between experimental data and theoretical models.