Related Experiment Video
Updated: Jul 19, 2026

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
Published on: November 29, 2013
The random walk description for isotope exchange in a polypeptide
1Department of Applied Physics, Waseda University, Okubo, Tokyo 160, Japan.
Abstract:
Isotope exchange in a polypeptide is considered from the point of view in which the boundary point between helix and coil regions of a polypeptide behaves like a weakly asymmetric random walker. We assume that the boundary point is reflected completely at the ends of a polypeptide. The equilibrium fraction of helix region is obtained under this assumption, and this is also confirmed by computer simulation. The experimental results of isotope exchange can be explained in this situation. On the other hand. the rate constant of exchange of a residue given by experiments can also be explained by another assumption, as considered before (M. Fujiwara and N. Saitô, Polym. J. 9 (1977) 625.), in which the nucleations of coil states take place in the helix region. Which of the two is of major importance is left to further studies.
More Related Videos
09:18Time-resolved ElectroSpray Ionization Hydrogen-deuterium Exchange Mass Spectrometry for Studying Protein Structure and Dynamics
Published on: April 17, 2017
10:31Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
Published on: February 3, 2022
Related Concept Videos
Ion Exchange
Post-translational Translocation of Proteins to the RER
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
Energy to Drive Translocation
Generally, polypeptides are unfolded by two distinct...
Peptide Bonds
Termination of Translation
Improving Translational Accuracy