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Oligosaccharide Assembly

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Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
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Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...

Amyloid Fibrils

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
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Protein Complex Assembly

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Related Experiment Video

Updated: Jul 2, 2026

Self-assembly of Complex Two-dimensional Shapes from Single-stranded DNA Tiles

Self-assembly of Complex Two-dimensional Shapes from Single-stranded DNA Tiles

Published on: May 8, 2015

Cross-strand pairing and amyloid assembly.

Yan Liang¹, Sai Venkatesh Pingali, Ashutosh S Jogalekar

¹Center for Fundamental and Applied Molecular Evolution, Department of Chemistry, Emory University, Atlanta, Georgia 30322, USA.

|September 2, 2008

Summary

Researchers studied Alzheimer's disease peptides (Abeta) to understand how amino acid interactions stabilize protein structures. They found that specific cross-strand pairings and a desolvation step are critical for amyloid assembly.

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Area of Science:

Biochemistry
Structural Biology
Neuroscience

Background:

Amino acid cross-strand pairing influences protein beta-sheet assembly and stability.
Direct evaluation of these interactions in amyloid formation has been challenging.

Purpose of the Study:

To develop an experimental system using the Abeta(16-22) peptide to evaluate cross-strand pairing interactions in beta-sheet formation.
To investigate the roles of electrostatic and steric interactions in beta-sheet registry and amyloid assembly.

Main Methods:

Utilized the Abeta(16-22) peptide as a model system for internal comparisons of interactions.
Analyzed morphological transitions (fibers to nanotubes) as indicators of beta-strand registry.
Investigated the impact of beta-sequence and pair correlations on secondary assembly.

Main Results:

Demonstrated that cross-strand pairing interactions critically regulate beta-sheet surface complementarity and registry.
Observed a morphological transition linked to changes in beta-sheet surface complementarity.
Identified a critical desolvation step in amyloid assembly not typically included in current models.

Conclusions:

Cross-strand pairing interactions and beta-sequence correlations are essential for regulating protein beta-sheet assembly.
Amyloid formation involves a critical desolvation step influencing secondary structure and morphology.
The Abeta(16-22) peptide system effectively probes interactions governing beta-sheet registry and amyloidogenesis.