Related Experiment Video
Updated: Aug 13, 2026

Optical Tweezers to Study RNA-Protein Interactions in Translation Regulation
Published on: February 12, 2022
Relationships between the folding rate constant and the topological parameters of small two-state proteins based on
1Department of Physics, Dalian Maritime University, Dalian 116026, PR China. dongmi@dlut.edu.cn
Abstract:
In this paper, we propose an analytically tractable model of protein folding based on one-dimensional general random walk. A second-order differential equation for the mean folding time of a single protein is constructed which can be used to derive the observed relationship between the folding rate constant and the number of native contacts. The parameters appearing in the model can be determined by fitting the theoretical prediction to the experimental result. In addition, taking into account the fact that the number of native contacts is almost proportional to the relative contact order, we can also explain the observed relationship between the folding rate constant and the relative contact order.
More Related Videos
09:17Structure-Based Simulation and Sampling of Transcription Factor Protein Movements along DNA from Atomic-Scale Stepping to Coarse-Grained Diffusion
Published on: March 1, 2022
09:25NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
Published on: November 1, 2024
Related Concept Videos
Protein Folding
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding
Noncovalent Attractions in Biomolecules
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,...
Molecular Chaperones and Protein Folding
The...
Cooperative Allosteric Transitions