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ノンコヴァラント・ダイメリゼーションの分子工学

  • 0State Key Laboratory of Supramolecular Structure and Materials, College of Chemistry, Jilin University, Changchun 130012, China.

まとめ

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Noncovalent Attractions in Biomolecules 02:35

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Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...

Cooperative Binding of Transcription Regulators 02:13

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Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome.  Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form...

Cooperative Allosteric Transitions 01:58

8.0K

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...

Protein-protein Interfaces 02:04

12.7K

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...

Van der Waals Interactions 01:24

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Atoms and molecules interact with each other through intermolecular forces. These electrostatic forces arise from attractive or repulsive interactions between particles with permanent, partial, or temporary charges. The intermolecular forces between neutral atoms and molecules are ion–dipole, dipole–dipole, and dispersion forces, collectively known as van der Waals forces.

Polar molecules have a partial positive charge on one end and a partial negative charge on the other end of...

Molecular Geometry and Dipole Moments 02:36

13.7K

The VSEPR theory can be used to determine the electron pair geometries and molecular structures as follows:

Write the Lewis structure of the molecule or polyatomic ion.
Count the number of electron groups (lone pairs and bonds) around the central atom. A single, double, or triple bond counts as one region of electron density.
Identify the electron-pair geometry based on the number of electron groups.
Use the number of lone pairs to determine the molecular structure. If more than one...