Characterization of the folding and unfolding reactions of a small β-barrel protein of novel topology, the MTCP1 oncogene product P13

C Roumestand, M Boyer, L Guignard, P Barthe… - Journal of Molecular …, 2001 - Elsevier
The equilibrium and kinetic folding properties of a small oncogene product, P13MTCP1, of
novel topology have been investigated using perturbation by guanidine hydrochloride and …

Differential stabilization of two hydrophobic cores in the transition state of the villin 14T folding reaction

SE Choe, L Li, PT Matsudaira, G Wagner… - Journal of Molecular …, 2000 - Elsevier
We report the distribution of hydrophobic core contacts during the folding reaction transition
state for villin 14T, a small 126-residue protein domain. The solution structure of villin 14T …

Protein contact order prediction from primary sequences

Y Shi, J Zhou, D Arndt, DS Wishart, G Lin - BMC bioinformatics, 2008 - Springer
Background Contact order is a topological descriptor that has been shown to be correlated
with several interesting protein properties such as protein folding rates and protein transition …

The importance of explicit chain representation in protein folding models: An examination of Ising‐like models

J Karanicolas, CL Brooks III - Proteins: Structure, Function, and …, 2003 - Wiley Online Library
A class of models that represents a protein chain as a sequence of “folded” and “unfolded”
residues has recently been used to correlate rates and mechanisms of protein folding with …

Roles of physical interactions in determining protein‐folding mechanisms: Molecular simulation of protein G and α spectrin SH3

S Yup Lee, Y Fujitsuka, DH Kim… - … : Structure, Function, and …, 2004 - Wiley Online Library
Protein‐folding mechanisms of two small globular proteins, IgG binding domain of protein G
and α spectrin SH3 domain are investigated via Brownian dynamics simulations with a …

Interaction between Two Discontiguous Chain Segments from the β-Sheet of Escherichia coli Thioredoxin Suggests an Initiation Site for Folding

ML Tasayco, J Fuchs, XM Yang, D Dyalram… - Biochemistry, 2000 - ACS Publications
The approach of comparing folding and folding/binding processes is exquisitely poised to
narrow down the regions of the sequence that drive protein folding. We have dissected the …

Extending the folding nucleus of ubiquitin with an independently folding β-hairpin finger: hurdles to rapid folding arising from the stabilisation of local interactions

R Bofill, ER Simpson, GW Platt, MD Crespo… - Journal of molecular …, 2005 - Elsevier
The N-terminal β-hairpin sequence of ubiquitin has been implicated as a folding nucleation
site. To extend and stabilise the ubiquitin folding nucleus, we have inserted an …

Hydrogen bonds, hydrophobicity forces and the character of the collapse transition

A Irbäck, F Sjunnesson, S Wallin - Journal of Biological Physics, 2001 - Springer
We study the thermodynamic behavior of a model protein with 54 amino acidsthat is
designed to form a three-helix bundle in its native state. The model contains three types of …

Quantitative description and classification of protein structures by a novel robust amino acid network: interaction selective network (ISN)

S Konno, T Namiki, K Ishimori - Scientific Reports, 2019 - nature.com
To quantitatively categorize protein structures, we developed a quantitative coarse-grained
model of protein structures with a novel amino acid network, the interaction selective …

Characterization of architecture signals in proteins

S Rackovsky - The Journal of Physical Chemistry B, 2006 - ACS Publications
A quantitative, property-based approach to protein sequence analysis is presented,
grounded in Fourier analysis and signal-processing methodologies. The resulting tools are …