Hydrophobic Core
Hydrophobic Core - Related Videos
02:10
The Nucleosome Core Particle
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2020
Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins. The paradox Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their main responsibility is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. While on the other hand, they must allow polymerase enzymes to access DNA...
03:22
Calcium-Dependent Hydrophobic Interaction Chromatography: A Technique to Purify Calcium-Binding Proteins Based on Hydrophobic Interactions
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2025
In this video, we demonstrate the purification of calcium-binding protein from a dialyzed cell lysate through calcium-dependent hydrophobic interaction chromatography. The calcium-binding proteins expose a hydrophobic region upon binding with calcium, facilitating interaction with a hydrophobic group on resin. Later these proteins are eluted using calcium chelator EDTA that reverses the interaction.
03:46
Butyl-Dependant Hydrophobic Interaction Liquid Chromatography: A Technique to Characterize Antibody-Drug Conjugates Based on Hydrophobic Interactions
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2025
This video demonstrates the hydrophobic interaction liquid chromatography-based characterization of antibody-drug conjugates. Using a butyl ligand-based chromatography column, the antibody-drug conjugates are characterized via hydrophobic interactions with the ligand.
11:16
Hydrophobic Salt-modified Nafion for Enzyme Immobilization and Stabilization
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Cited by 23 •
2012
This article will describe the procedure for synthesizing a hydrophobically modified Nafion enzyme immobilization membrane and how to immobilize proteins and/or enzymes within the membrane and test their specific activity.
02:23
Visualizing the Effect of pH on Solubilization of the Influenza A Viral Core
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2026
Source: Stauffer, S. et al., In Vitro Disassembly of Influenza A Virus Capsids by Gradient Centrifugation. J. Vis. Exp. (2016)This video demonstrates the effect of pH on the solubilization of influenza A viral cores. Gel electrophoresis and protein staining reveal the progressive disassembly of the core structure under acidic conditions.
FAQs
These residues have nonpolar side chains that interact poorly with water. Folding brings them together inside the protein, reducing the amount of nonpolar surface exposed to the surrounding environment. Their clustering also creates a compact interior that supports the protein’s three-dimensional arrangement, making hydrophobic residue placement an important factor in conformational stability.
Buried nonpolar residues provide much of the core’s packing, while nearby polar groups add stabilizing interactions. In particular, polar groups can form hydrogen bonds and other interactions that reinforce the folded arrangement. This cooperation matters because core stability depends not only on excluding water, but also on how surrounding chemical groups are organized within the protein structure.
A substitution can alter how efficiently nonpolar side chains cluster or how well neighboring groups fit together. Such a change may reduce conformational stability, disturb the protein’s three-dimensional structure, or promote misfolding. Examining these effects helps connect a specific sequence change with altered protein behavior rather than treating every substitution as equivalent.
The identity and placement of nonpolar amino acids help constrain how a protein folds into a three-dimensional form. When these residues pack appropriately, the resulting interior supports a stable conformation; when their arrangement changes, folding can be disrupted. This makes core organization a useful link between amino acid sequence, structure, and stability.
Core analysis can reveal how a protein’s internal arrangement supports its conformation and how substitutions affect that arrangement. Researchers can use these principles to interpret structural changes, assess possible effects on stability, and investigate why altered packing may be associated with misfolding. The approach therefore connects molecular structure with experimentally relevant protein behavior.
In protein engineering, these principles help guide attention toward substitutions that may change internal packing, conformational stability, or folding behavior. In disease-mechanism research, the same reasoning helps examine how sequence changes could promote misfolding. Together, these applications use core organization to relate molecular alterations to changes in protein structure and function.