Related Experiment Video
Updated: Jan 21, 2026
19:50
Interview: Protein Folding and Studies of Neurodegenerative Diseases
Published on: July 16, 2008
13.2K
Weak Chemical Interactions That Drive Protein Evolution: Crowding, Sticking, and Quinary Structure in Folding and
Drishti Guin1, Martin Gruebele1,2,3
1Department of Chemistry , University of Illinois , Urbana , Illinois 61801 , United States.
Chemical Reviews
|July 30, 2019
Summary
Cellular biomolecule dynamics are influenced by their environment, affecting stability and function. Understanding these interactions, including crowding and quinary structure, is key to protein evolution and biological system organization.
Area of Science:
- Biophysics
- Cell Biology
- Evolutionary Biology
Background:
- Advances in instrumentation and computing power allow imaging of biomolecular dynamics within cells.
- Understanding the chemical organization of biological systems relies on studying these dynamics.
- Biomolecular behavior is context-dependent, varying with cell cycle, location, and stress.
Purpose of the Study:
- To review cellular interactions affecting biomolecular stability and function.
- To detail crowding, sticking, and quinary structure and their quantification.
- To discuss protein evolution in cells using biophysical evidence.
Main Methods:
- Review of current literature on cellular biomolecular dynamics.
- Description of in vitro and in vivo methods for quantifying crowding, sticking, and quinary structure.
- Analysis of biophysical evidence related to protein evolution.
Main Results:
- Cellular environment significantly modulates biomolecular stability and function.
- Crowding, sticking, and quinary structure are critical factors influencing biomolecular behavior.
- Protein interactions shape evolutionary pathways by affecting free energy and epistasis.
Conclusions:
- Cellular context is crucial for understanding biomolecular behavior and evolution.
- Biophysical insights provide a framework for studying protein evolution and interaction networks.
- Future research requires collaboration between evolutionary biology and biophysics.
Related Concept Videos
01:22Protein Folding
126.7K
Overview
126.7K
01:25Protein Folding
11.2K
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 Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
11.2K
01:56Structural Protein Function
29.8K
Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to...
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to...
29.8K
01:56Structural Protein Function
3.2K
3.2K
03:00Molecular Chaperones and Protein Folding
19.7K
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
The...
19.7K
02:15Protein and Protein Structure
87.0K
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...
A protein's shape is critical to its function. For example, an enzyme...
87.0K