Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Protein and Protein Structure

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...

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

Protein Organization

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-protein Interfaces

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Biologically Younger Individuals, as Identified by MARK-AGE Biological Age Scores, Display a Distinct Favourable Blood Chemistry Profile Regardless of Age.

Aging cell·2026

Same author

Development of Ferrero Nutrition Criteria: category-specific, progressive guidelines for product innovation.

Frontiers in nutrition·2025

Same author

Circulating cell-free DNA in health and disease - the relationship to health behaviours, ageing phenotypes and metabolomics.

GeroScience·2022

Same author

Whole-genome sequencing analysis of semi-supercentenarians.

eLife·2021

Same author

Genomic history of the Italian population recapitulates key evolutionary dynamics of both Continental and Southern Europeans.

BMC biology·2020

Same author

Intracrystalline incorporation of nacre protein hydrogels modifies the mechanical properties of calcite crystals: a microcompression study.

Journal of materials chemistry. B·2020

Search research articles

Related Experiment Video

Updated: Jul 16, 2026

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

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

Published on: May 13, 2020

Structural features that distinguish kinetically distinct biomineralization polypeptides.

Sebastiano Collino¹, John Spencer Evans

¹Center for Biomolecular Materials Spectroscopy, Laboratory for Chemical Physics, New York University, 345 East 24th Street, New York, New York 10010, USA.

Biomacromolecules

|March 27, 2007

Summary

Pacific red abalone shell proteins AP7 and AP24 share mineralization roles. Protein AP24N exhibits enhanced kinetics due to its planar structure and longer anionic/hydrogen-bonding sequences, facilitating faster crystal formation.

More Related Videos

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

Insights into the Interactions of Amino Acids and Peptides with Inorganic Materials Using Single-Molecule Force Spectroscopy

Insights into the Interactions of Amino Acids and Peptides with Inorganic Materials Using Single-Molecule Force Spectroscopy

Published on: March 6, 2017

Related Experiment Videos

Last Updated: Jul 16, 2026

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

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

Published on: May 13, 2020

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

Insights into the Interactions of Amino Acids and Peptides with Inorganic Materials Using Single-Molecule Force Spectroscopy

Insights into the Interactions of Amino Acids and Peptides with Inorganic Materials Using Single-Molecule Force Spectroscopy

Published on: March 6, 2017

Area of Science:

Biomineralization
Materials Science
Structural Biology

Background:

Pacific red abalone shell proteins AP7 and AP24 are crucial for aragonite formation in nacre.
The N-terminal domains (AP7N, AP24N) show similar mineralization capabilities in vitro but differ in kinetics (AP24N > AP7N).

Purpose of the Study:

To identify novel molecular features of AP24N.
To contrast the lowest energy structures of AP24N and AP7N.
To elucidate the structural basis for AP24N's enhanced mineralization kinetics.

Main Methods:

Nuclear Magnetic Resonance (NMR) spectroscopy.
Simulated annealing molecular dynamics simulations.
Analysis of protein conformation, ion binding, and surface properties.

Main Results:

AP24N and AP7N share unfolded conformations, Ca(II) sequestration, calcite adsorption, and electrostatic pockets.
AP24N exhibits greater Ca(II) responsiveness, a more planar backbone, and longer anionic/hydrogen-bonding sequence blocks compared to AP7N.
AP7N adopts a 'bent paper clip' configuration, while AP24N favors a planar configuration.

Conclusions:

Unfolded conformation, electrostatic pockets, and sequence clustering contribute to AP7N and AP24N's similar mineralization effects.
AP24N's unique features (longer charged/H-bonding blocks, planar structure) enhance its mineralization kinetics over AP7N.
These structural differences facilitate peptide-mineral, peptide-ion, and water cluster interactions, driving faster biomineralization.