Microscopic derivation of the low-T myoglobin-CO recombination rate law by estimating statistical parameters of folding relaxation
Author:
Publisher
Wiley
Subject
General Chemical Engineering
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1002/bbpc.19940980222/fullpdf
Reference9 articles.
1. Dynamics of ligand binding to myoglobin
2. The Energy Landscapes and Motions of Proteins
3. Temperature-dependent X-ray diffraction as a probe of protein structural dynamics
4. Intermediates and barrier crossing in a random energy model (with applications to protein folding)
5. Relaxation to Equilibrium in the Random Energy Model
Cited by 5 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Energy-level statistics in the fine conformational resolution of RNA folding dynamics;Physical Review E;1999-11-01
2. How large should proteins be? The minimal size of a good structure seeker;Physical Chemistry Chemical Physics;1999
3. Adiabatic ansatz in RNA folding dynamics;Physical Review E;1997-07-01
4. Variational Approach to Relaxation in Complex Free Energy Landscapes: The Polymer Folding Problem;Physical Review Letters;1997-03-31
5. Statistical folding dynamics for random heteropolymers;Journal of Physics A: Mathematical and General;1996-10-21
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