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Why fibrous proteins are romantic

¹Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, Massachusetts, 02254-9110, USA.

Journal of Structural Biology

|September 2, 1998

Summary

This personal account traces the history of fibrous protein structure, from early diffraction studies to atomic resolution. Key insights reveal helical coils, beta-sheets, and collagen

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Area of Science:

Structural biology
Biophysics
Molecular biology

Background:

Historical overview of fibrous protein structure research, starting with Astbury's foundational work.
Deciphering of X-ray diffraction patterns by Pauling, Crick, and Ramachandran to elucidate alpha-helical coiled coils, beta-sheets, and collagen's triple helix.
Identification of local and long-range sequence periodicities (magic numbers) explaining axial repeats in fibrous protein filaments.

Discussion:

Advancements in fibrous protein structure analysis to atomic resolution.
Leucine zippers as models for protein design, offering insights beyond globular proteins.
Exploration of fibrous protein dynamics, including viral fusion mechanisms and prion protein conformational changes.

Key Insights:

Fibrous proteins exhibit diverse structural motifs like alpha-helical coiled coils and beta-sheets.
Sequence periodicities are critical determinants of fibrous protein filament structure and axial repeats.
Atomic resolution studies and dynamic analyses are deepening the understanding of fibrous protein function and design.

Outlook:

Continued investigation into the dynamic mechanisms of fibrous proteins.
Potential links between fibrous and globular protein conformational changes, as seen in prion diseases.
Application of fibrous protein insights to broader protein design principles.

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