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Related Concept Videos

Conservation of Protein Domains Over Different Proteins02:26

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.
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Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...
Conservation of Protein Domains02:26

Conservation of Protein Domains

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...
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Protein Organization

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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 Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
09:51

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Published on: July 16, 2017

MORPH-PRO: a novel algorithm and web server for protein morphing.

Natalie E Castellana1, Andrey Lushnikov, Piotr Rotkiewicz

  • 1Algorithmic Biology Laboratory, Saint Petersburg Academic University, Saint Petersburg, Russia. kira@math.spbu.ru.

Algorithms for Molecular Biology : AMB
|July 13, 2013
PubMed
Summary
This summary is machine-generated.

Computational protein morphing visualizes dynamic protein conformational changes. The novel Morph-Pro algorithm generates accurate intermediate structures for improved protein-ligand docking and virtual screening.

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Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins
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An Integrated Approach for Microprotein Identification and Sequence Analysis
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An Integrated Approach for Microprotein Identification and Sequence Analysis

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Last Updated: May 9, 2026

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Application of I TASSER, trRosetta, UCSF Chimera, HADDOCK server, and HEX loria for De Novo and In Silico Design of Proteins
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An Integrated Approach for Microprotein Identification and Sequence Analysis
09:37

An Integrated Approach for Microprotein Identification and Sequence Analysis

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Area of Science:

  • Structural biology
  • Computational biology
  • Biophysics

Background:

  • Proteins are dynamic molecules, transitioning between conformations to perform cellular functions.
  • Experimental methods capture only static snapshots, limiting understanding of protein dynamics.
  • Computational protein morphing generates intermediate structures to visualize conformational changes.

Purpose of the Study:

  • To introduce a novel and efficient protein morphing algorithm, Morph-Pro.
  • To demonstrate the utility of generated intermediate structures beyond visualization.
  • To assess the potential of these structures in molecular modeling and virtual screening.

Main Methods:

  • Developed Morph-Pro, an algorithm based on linear interpolation for protein morphing.
  • Utilized intermediate structures from a c-Jun N-terminal kinase (JNK1) conformational change.
  • Performed virtual docking experiments using these intermediate structures.

Main Results:

  • Morph-Pro efficiently generates intermediate protein conformations.
  • Intermediate structures from JNK1 conformational change docked with higher scores to known ligands compared to X-ray structures.
  • This highlights the potential of computationally derived structures in modeling and screening.

Conclusions:

  • Protein conformational change visualization is crucial for understanding protein function.
  • Morph-Pro-generated intermediate structures are accurate approximations of true structures.
  • Computationally predicted structures show promise for protein-ligand docking and virtual screening applications.