@Article{CiCP-7-2,
author = {},
title = {Transition States in Protein Folding},
journal = {Communications in Computational Physics},
year = {2010},
volume = {7},
number = {2},
pages = {283--300},
abstract = {<p style="text-align: justify;">The folding dynamics of small single-domain proteins is a current focus of
simulations and experiments. Many of these proteins are &#39;two-state folders&#39;, i.e. proteins
that fold rather directly from the denatured state to the native state, without populating
metastable intermediate states. A central question is how to characterize the
instable, partially folded conformations of two-state proteins, in particular the rate-limiting
transition-state conformations between the denatured and the native state.
These partially folded conformations are short-lived and cannot be observed directly
in experiments. However, experimental data from detailed mutational analyses of the
folding dynamics provide indirect access to transition states. The interpretation of
these data, in particular the reconstruction of transition-state conformations, requires
simulation and modeling. The traditional interpretation of the mutational data aims
to reconstruct the degree of structure formation of individual residues in the transition
state, while a novel interpretation aims at degrees of structure formation of cooperative
substructures such as α-helices and β-hairpins. By splitting up mutation-induced free
energies into secondary and tertiary structural components, the novel interpretation
resolves some of the inconsistencies of the traditional interpretation.</p>},
issn = {1991-7120},
doi = {https://doi.org/10.4208/cicp.2009.08.202},
url = {https://global-sci.com/article/80979/transition-states-in-protein-folding}
}