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Related Concept Videos

Protein Folding01:22

Protein Folding

Overview
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Organization01:13

Protein Organization

Overview
Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.
Protein and Protein Structure02:15

Protein and Protein Structure

Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...
Newman Projections02:06

Newman Projections

Different notations are used to represent the three-dimensional structure of molecules on two-dimensional surfaces. One of the most commonly used representations is the dash-wedge formula. The dashed wedges, solid wedges, and the plane lines indicate the groups situated behind the plane, coming out of the plane, and in the plane, respectively.
The organic molecules rotate across the single bonds leading to numerous temporary three-dimensional structures of varying energy known as conformers.

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Related Experiment Video

Updated: Jun 26, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
11:27

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

A new artificial beta-sheet that dimerizes through parallel beta-sheet interactions.

Sergiy Levin1, James S Nowick

  • 1Department of Chemistry, University of California, Irvine, Irvine, California 92697-2025, USA.

Organic Letters
|January 29, 2009
PubMed
Summary
This summary is machine-generated.

Researchers developed a chemical model for beta-sheet dimerization. This model, using linked dipeptides, demonstrates soluble and stable beta-sheet interactions relevant to protein aggregates.

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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

Related Experiment Videos

Last Updated: Jun 26, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
11:27

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
14:55

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

Area of Science:

  • Biochemistry
  • Chemical Biology
  • Molecular Biology

Background:

  • Beta-sheet structures are crucial in protein folding and aggregation.
  • Understanding the fundamental interactions of beta-sheets is key to studying protein misfolding diseases.
  • Soluble models are needed to investigate these interactions effectively.

Purpose of the Study:

  • To design and characterize a novel chemical model system for studying parallel beta-sheet dimerization.
  • To demonstrate the utility of a templated, linked dipeptide system for mimicking protein aggregate interactions.
  • To provide a soluble and tractable system for investigating beta-sheet assembly.

Main Methods:

  • Chemical synthesis of a model system comprising two C-terminally linked dipeptides attached to a molecular template.
  • Proton Nuclear Magnetic Resonance ((1)H NMR) spectroscopy to confirm beta-sheet folding and dimerization in CDCl(3) solution.

Main Results:

  • Successful synthesis and characterization of the chemical model.
  • (1)H NMR data confirmed the formation of a stable beta-sheet structure.
  • The model system demonstrated dimerization through parallel beta-sheet interactions in solution.

Conclusions:

  • Linking peptide strands and blocking assembly edges yields soluble, stable beta-sheet systems.
  • This model system effectively mimics interactions found in larger peptide and protein aggregates.
  • The developed system offers a valuable tool for studying the fundamental principles of beta-sheet formation and aggregation.