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Protein Folding

Protein Folding

Protein Folding

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 Organization

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 Organization

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Amyloid Fibrils

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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,...

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Related Experiment Video

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Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

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Published on: September 12, 2019

Emerging Methods for Structural Analysis of Protein Aggregation.

Eshan Khan, Subodh K Mishra, Amit Kumar¹

¹Centre for Biosciences and Biomedical Engineering, Indian Institute of Technology, Indore 452017, Madhya Pradesh. India.

Protein and Peptide Letters

|February 9, 2017

Summary

Understanding protein misfolding and aggregation is crucial for neurodegenerative disease therapeutics. This review highlights spectroscopic methods to analyze protein structures and aggregation pathways for better drug design.

Keywords:

NMR spectroscopy Neurodegenerative diseases amyloid like proteins circular dichroism fluorescence spectroscopy protein aggregation raman spectroscopy

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Area of Science:

Neuroscience
Biochemistry
Structural Biology

Background:

Protein misfolding and aggregation are hallmarks of neurodegenerative diseases.
Intrinsically disordered proteins associated with these diseases pose challenges for structure-based drug design.
Characterizing misfolded proteins and their aggregation pathways is essential for developing effective therapeutics.

Purpose of the Study:

To review spectroscopic methods for analyzing protein aggregation.
To elucidate the structural role of intermediate steps in protein aggregation.
To advance therapeutic strategies for protein misfolding-related neurological diseases.

Main Methods:

Fluorescence spectroscopy
Circular Dichroism (CD) spectroscopy
Nuclear Magnetic Resonance (NMR) spectroscopy
Fourier Transform Infrared (FTIR) spectroscopy
Raman spectroscopy

Main Results:

Spectroscopic methods provide insights into the structural analysis of protein aggregation.
Understanding invisible intermediates in protein aggregation is key.
These methods aid in discerning conformational roles and involved pathways during aggregation.

Conclusions:

Structural analysis of protein aggregation using biophysical methods can improve therapeutics.
Elucidating intermediate steps in protein aggregation is vital for drug development.
Advancing the understanding of misfolded proteins and aggregation mechanisms can target neurological diseases more effectively.