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Related Concept Videos

Mechanical Protein Functions

Mechanical Protein Functions

Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical forces and proteins that are subjected to mechanical forces. Proteins providing mechanical support to the structure of the cell, such as keratin, are subjected to mechanical force, whereas proteins involved in cell movement and transport of molecules across cell membranes, such as an ion pump, are examples of generating mechanical force.

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 Folding

Protein Folding

Protein Folding

Protein Folding

Protein Denaturation

Protein Denaturation

The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...

Covalently Linked Protein Regulators

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.

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Related Experiment Video

Updated: Jul 5, 2026

High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States

High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States

Published on: June 29, 2021

Conformational changes in protein function.

Haiguang Liu¹, Shubhra Ghosh Dastidar, Hongxing Lei

¹Genome Center, University of California, Davis, CA, USA.

Methods in Molecular Biology (Clifton, N.J.)

|May 1, 2008

Summary

This summary is machine-generated.

Protein dynamics are crucial for function. Molecular dynamics (MD) simulations offer detailed insights into protein conformational changes, with advanced techniques enhancing sampling efficiency.

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Area of Science:

Biophysics
Computational Biology

Background:

Protein conformational changes are fundamental to protein dynamics and function.
Molecular dynamics (MD) simulation is a key computational method for studying protein structure at atomic resolution over time.

Purpose of the Study:

To review the applications of MD simulations in understanding protein conformational changes.
To introduce advanced sampling techniques like locally enhanced sampling (LES) and grow-to-fit molecular dynamics (G2FMD).

Main Methods:

Utilizing molecular dynamics (MD) simulations to analyze protein structural dynamics.
Applying advanced sampling methods (LES, G2FMD) to improve simulation efficiency.

Main Results:

MD simulations provide atomic-level insights into time-resolved protein structural properties.
Advanced techniques like LES and G2FMD enhance the efficiency of sampling protein conformational landscapes.

Conclusions:

MD simulations are versatile tools for studying protein conformational changes.
Advanced sampling techniques are crucial for overcoming limitations in simulating complex protein dynamics.