Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

The Water Cycle01:00

The Water Cycle

The Earth’s hydrosphere includes all of the areas where the storage and movement of water occurs. Since water is the basis of all living processes, the cycling of water is extremely important to ecosystem dynamics.
Role of Water in Human Biology01:27

Role of Water in Human Biology

Water is the one of the most significant components of the human body; it plays a crucial role in several physiological activities because of its unique physicochemical properties. Importantly, it helps to regulate body temperature and is the chief component of several body fluids.
Water's Solvent Properties
Since water is a polar molecule with slightly positive and slightly negative charges, ions and polar molecules can readily dissolve in it. Therefore, it is referred to as a solvent, a...
States of Water01:23

States of Water

Water exists in any one of the three classical states: solid (ice), liquid (water), and gas (steam or water vapor). The state of water depends on i) the intermolecular forces that draw molecules together and ii) the kinetic energy that leads to movements that pull them apart.
Water freezes when the intermolecular forces are greater than the kinetic energy. Unlike most other substances, water is less dense in its solid state than in its liquid state. This is because each water molecule can form...
Aquaporins01:25

Aquaporins

Aquaporins or AQPs are a family of integral membrane proteins whose primary function is to transport water, while some called aquaglyceroporins also transport glycerol. In addition, aquaporins have also been suspected to be involved in transporting volatile substances, such as carbon dioxide and ammonia, across membranes. Such AQPs that act as gas channels are often highly expressed in cells involved in the gaseous exchange, such as red blood cells, epithelial cells, and pulmonary capillaries.
Pascal's Law01:04

Pascal's Law

In 1653, the French philosopher and scientist Blaise Pascal published "Treatise on the Equilibrium of Liquids," which discussed the principles of static fluids. A static fluid is a fluid that is not in motion. When a fluid is not flowing, we say that the fluid is in static equilibrium. If the fluid is water, we say it is in hydrostatic equilibrium. For a fluid in static equilibrium, the net force on any part of the fluid must be zero; otherwise, the fluid will start to flow. Pascal observed...
Cohesion01:07

Cohesion

Cohesion is the attraction between molecules of the same type, such as water molecules. Water molecules have an overall neutral charge but are polar molecule. An oxygen atom in one water molecule has a partial negative charge that can bind to a hydrogen atom with a partial positive charge in a second water molecule, forming a hydrogen bond. Each water molecule can form up to four hydrogen bonds with other water molecules. Hydrogen bonds are responsible for water's cohesive nature.
On a surface,...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Synthesis of uniformly deuterated n-dodecyl-β-D-maltoside (d39-DDM) for solubilization of membrane proteins in TROSY NMR experiments.

Journal of labelled compounds & radiopharmaceuticals·2014
Same author

TROSY NMR with a 52 kDa sugar transport protein and the binding of a small-molecule inhibitor.

Molecular membrane biology·2014
Same author

¹H, ¹⁵N, and ¹³C backbone chemical shift assignment of titin domains A59-A60 and A60 alone.

Biomolecular NMR assignments·2014
Same author

Ribosome clearance by FusB-type proteins mediates resistance to the antibiotic fusidic acid.

Proceedings of the National Academy of Sciences of the United States of America·2012
Same author

Ligand binding to distinct states diverts aggregation of an amyloid-forming protein.

Nature chemical biology·2011
Same author

¹H, ¹⁵N and ¹³C backbone chemical shift assignment of the titin A67-A68 domain tandem.

Biomolecular NMR assignments·2011

Related Experiment Video

Updated: Jul 13, 2026

Impacts of Free-falling Spheres on a Deep Liquid Pool with Altered Fluid and Impactor Surface Conditions
08:49

Impacts of Free-falling Spheres on a Deep Liquid Pool with Altered Fluid and Impactor Surface Conditions

Published on: February 17, 2019

Water, water everywhere--except where it matters?

Steve W Homans1

  • 1Astbury Centre for Structural Molecular Biology, University of Leeds LS2 9JT, UK. s.w.homans@leeds.ac.uk

Drug Discovery Today
|July 17, 2007
PubMed
Summary

Molecular binding affinity is not driven by solvent expulsion but by favorable dispersion interactions from suboptimal hydration. Optimizing shape complementarity can dramatically enhance binding by maximizing these solute-solute dispersion forces.

More Related Videos

Design and Fabrication of an Optical Fiber Made of Water
08:06

Design and Fabrication of an Optical Fiber Made of Water

Published on: November 8, 2018

Fat-Water Phantoms for Magnetic Resonance Imaging Validation: A Flexible and Scalable Protocol
07:59

Fat-Water Phantoms for Magnetic Resonance Imaging Validation: A Flexible and Scalable Protocol

Published on: September 7, 2018

Related Experiment Videos

Last Updated: Jul 13, 2026

Impacts of Free-falling Spheres on a Deep Liquid Pool with Altered Fluid and Impactor Surface Conditions
08:49

Impacts of Free-falling Spheres on a Deep Liquid Pool with Altered Fluid and Impactor Surface Conditions

Published on: February 17, 2019

Design and Fabrication of an Optical Fiber Made of Water
08:06

Design and Fabrication of an Optical Fiber Made of Water

Published on: November 8, 2018

Fat-Water Phantoms for Magnetic Resonance Imaging Validation: A Flexible and Scalable Protocol
07:59

Fat-Water Phantoms for Magnetic Resonance Imaging Validation: A Flexible and Scalable Protocol

Published on: September 7, 2018

Area of Science:

  • Biophysics
  • Molecular Biology
  • Computational Chemistry

Background:

  • Biological processes rely on precise molecular recognition with specific binding affinities.
  • Accurately computing binding affinities from molecular structures remains a significant challenge.
  • Biophysical techniques allow the thermodynamic contributions of protein, ligand, and solvent to binding to be analyzed.

Purpose of the Study:

  • To investigate the driving forces behind molecular binding affinity in a model protein system.
  • To explore the role of solvent interactions and dispersion forces in protein-ligand binding.
  • To identify strategies for enhancing binding affinity through molecular design.

Main Methods:

  • Utilized modern biophysical techniques to decompose binding thermodynamics.
  • Studied a model protein with a hydrophobic binding pocket.
  • Analyzed contributions from protein, cognate ligand, and solvent to binding affinity.

Main Results:

  • Binding affinity is primarily driven by favorable dispersion interactions, not the entropic loss of solvent.
  • Suboptimal hydration of the protein-binding pocket contributes positively to binding affinity.
  • Dispersion interactions arise from the protein-binding pocket's interaction with the ligand.

Conclusions:

  • Binding affinity is governed by dispersion interactions, particularly in cases of suboptimal hydration.
  • Shape complementarity is a key factor for optimizing solute-solute dispersion interactions.
  • Enhancing binding affinity can be achieved by maximizing favorable dispersion forces and minimizing opposing solute-solvent interactions.