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Related Concept Videos

Protein-protein Interfaces02:04

Protein-protein Interfaces

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 polypeptide...
Protein Folding01:22

Protein Folding

Overview
Protein Folding01:25

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...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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...
Noncovalent Attractions in Biomolecules02:35

Noncovalent Attractions in Biomolecules

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,...
Membrane Fluidity01:23

Membrane Fluidity

Cell membranes are composed of phospholipids, proteins, and carbohydrates loosely attached to one another through chemical interactions. Molecules are generally able to move about in the plane of the membrane, giving the membrane its flexible nature called fluidity. Two other features of the membrane contribute to membrane fluidity: the chemical structure of the phospholipids and the presence of cholesterol in the membrane.Fatty acids tails of phospholipids can be either saturated or...

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Updated: Jun 23, 2026

Single-Molecule Diffusion and Assembly on Polymer-Crowded Lipid Membranes
10:43

Single-Molecule Diffusion and Assembly on Polymer-Crowded Lipid Membranes

Published on: July 19, 2022

How interfaces affect hydrophobically driven polymer folding.

Sumanth N Jamadagni1, Rahul Godawat, Jonathan S Dordick

  • 1The Howard P. Isermann Department of Chemical & Biological Engineering and Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, New York 12180, USA.

The Journal of Physical Chemistry. B
|May 9, 2009
PubMed
Summary
This summary is machine-generated.

Hydrophobic polymer folding in water is significantly altered by interfaces. Interfaces reduce folding drive but accelerate folding kinetics, leading to distinct structures like pancake-like conformations or complete unfolding.

More Related Videos

Interfacial Molecular-level Structures of Polymers and Biomacromolecules Revealed via Sum Frequency Generation Vibrational Spectroscopy
09:43

Interfacial Molecular-level Structures of Polymers and Biomacromolecules Revealed via Sum Frequency Generation Vibrational Spectroscopy

Published on: August 13, 2019

Related Experiment Videos

Last Updated: Jun 23, 2026

Single-Molecule Diffusion and Assembly on Polymer-Crowded Lipid Membranes
10:43

Single-Molecule Diffusion and Assembly on Polymer-Crowded Lipid Membranes

Published on: July 19, 2022

Interfacial Molecular-level Structures of Polymers and Biomacromolecules Revealed via Sum Frequency Generation Vibrational Spectroscopy
09:43

Interfacial Molecular-level Structures of Polymers and Biomacromolecules Revealed via Sum Frequency Generation Vibrational Spectroscopy

Published on: August 13, 2019

Area of Science:

  • Polymer Science
  • Physical Chemistry
  • Biophysics

Background:

  • Hydrophobic interactions drive polymer folding in water, mirroring protein folding.
  • Water's structure, density, and fluctuations influence hydrophobic polymer folding kinetics.
  • Hydrophobic polymers exhibit interfacial activity, preferring interfaces over bulk water.

Purpose of the Study:

  • Investigate the impact of hydrophobic solid and vapor-water interfaces on polymer folding.
  • Analyze changes in structural, thermodynamic, and kinetic aspects of polymer folding at interfaces.
  • Compare interfacial effects to polymer folding in bulk water.

Main Methods:

  • Extensive molecular dynamics simulations were employed.
  • Simulations focused on hydrophobic polymers at solid-alkane-water and vapor-water interfaces.
  • Analysis included polymer structure, thermodynamics, and folding kinetics.

Main Results:

  • The hydrophobic driving force for polymer collapse decreases at solid-water and vapor-water interfaces.
  • Folded structures are marginally stable at solid-water interfaces, while vapor-water interfaces cause complete unfolding.
  • Polymer conformations become quasi-2D (pancake-like) at solid-water interfaces and are excluded from water at vapor-water interfaces.
  • Folding kinetics are faster at both interfaces despite reduced driving force.

Conclusions:

  • Hydrophobic interfaces significantly modify polymer folding thermodynamics and structure.
  • Water dynamics and fluctuations at hydrophobic interfaces accelerate folding kinetics.
  • Interface type (solid vs. vapor) dictates the extent of polymer unfolding and conformational changes.