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 Networks

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...

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.

Conserved Binding Sites

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...

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...

Gene Families

Gene Families

Gene families consist of groups of genes proposed to have originated from a common ancestor. Typically these arise through events in which a gene or genes are mistakenly duplicated during cell division. Unlike their parent genes (which are subject to selection pressure to maintain function), these gene copies do not need to preserve their sequences and may evolve at a relatively faster rate.
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...

Conservation of Protein Domains Over Different Proteins

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain. Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...

You might also read

Related Articles

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

Sort by

Same author

Bismuth drug as an antibiotic adjuvant to inhibit biofilm formation <i>via</i> a dual mechanism.

RSC medicinal chemistry·2026

Same author

A Soft Magnetic Jamming Method Enabling Variable Stiffness and Active Steering for Robotic Catheter.

Soft robotics·2026

Same author

The arsenic proteome in cancer: Unravelling molecular mechanisms of anticancer drugs.

Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry·2026

Same author

Medicinal applications of bismuth(III): from antimicrobial to anticancer.

Journal of inorganic biochemistry·2026

Same author

Unprecedented allosteric inhibition of <i>E. coli</i> malate dehydrogenase by silver(i) from atomic resolution analysis.

Chemical science·2025

Same author

Molecular Insights into Bismuth's New Applications against Antimicrobial Resistance and Coronaviruses.

Accounts of chemical research·2025

Search research articles

Related Experiment Video

Updated: May 10, 2026

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

Structure-oriented bioinformatic approach exploring histidine-rich clusters in proteins.

Shujian Cun¹, Yau-Tsz Lai, Yuen-Yan Chang

¹Department of Chemistry, The University of Hong Kong, Hong Kong, P.R. China.

Metallomics : Integrated Biometal Science

|June 18, 2013

Summary

Spatially clustered histidines (HrCs) in proteins are key for binding transition metals like zinc and copper. These histidine-rich clusters are linked to microbial pathogenesis, offering new avenues for drug design.

More Related Videos

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins

Published on: July 8, 2025

Related Experiment Videos

Last Updated: May 10, 2026

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins

Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins

Published on: July 8, 2025

Area of Science:

Biochemistry
Bioinformatics
Structural Biology

Background:

Histidines often appear in clusters within protein structures.
Histidine's coordination chemistry facilitates transition metal binding.
These clustered histidines (HrCs) are potentially crucial for protein function via metal interactions.

Purpose of the Study:

To identify and characterize histidine-rich clusters (HrCs) in proteins.
To investigate the role of HrCs in metal coordination.
To explore the functional implications of HrCs, particularly in relation to microbial pathogenesis.

Main Methods:

Bioinformatic analysis of protein sequences and structures.
Computational identification of histidine-rich clusters.
Correlation analysis between HrC proteins and known biological functions/interactions.

Main Results:

Over a thousand non-homologous HrC protein candidates were identified.
A significant proportion of identified HrCs interact with transition metals (Zn, Cu, Ni).
HrC proteins show correlations with microbial pathogenesis.

Conclusions:

Multiple histidines cluster to stabilize both static and dynamic metal binding.
HrCs are implicated in protein functions related to microbial pathogenesis.
This bioinformatic approach can be extended to study other amino acid-rich clusters and their structure-function relationships.