Three key residues form a critical contact network in a protein folding transition state

M Vendruscolo, E Paci, CM Dobson, M Karplus - Nature, 2001 - nature.com
Determining how a protein folds is a central problem in structural biology. The rate of folding
of many proteins is determined by the transition state, so that a knowledge of its structure is …

Ab initio protein structure prediction: progress and prospects

R Bonneau, D Baker - Annual review of biophysics and …, 2001 - annualreviews.org
▪ Abstract Considerable recent progress has been made in the field of ab initio protein
structure prediction, as witnessed by the third Critical Assessment of Structure Prediction …

Critical role of β-hairpin formation in protein G folding

EL McCallister, E Alm, D Baker - Nature structural biology, 2000 - nature.com
Abstract Comparison of the folding mechanisms of proteins with similar structures but very
different sequences can provide fundamental insights into the determinants of protein …

Protein folding theory: from lattice to all-atom models

L Mirny, E Shakhnovich - Annual review of biophysics and …, 2001 - annualreviews.org
▪ Abstract This review focuses on recent advances in understanding protein folding kinetics
in the context of nucleation theory. We present basic concepts such as nucleation, folding …

Protein folding transition path times from single molecule FRET

HS Chung, WA Eaton - Current opinion in structural biology, 2018 - Elsevier
Highlights•Single molecule FRET experiments determine average transition path
times.•Observed times are extremely close to those found in all-atom MD simulations.•Times …

[HTML][HTML] Inter-residue interactions in protein folding and stability

MM Gromiha, S Selvaraj - Progress in biophysics and molecular biology, 2004 - Elsevier
During the process of protein folding, the amino acid residues along the polypeptide chain
interact with each other in a cooperative manner to form the stable native structure. The …

Roles of native topology and chain-length scaling in protein folding: a simulation study with a Gō-like model

N Koga, S Takada - Journal of Molecular Biology, 2001 - Elsevier
We perform folding simulations on 18 small proteins with using a simple Gō-like protein
model and analyze the folding rate constants, characteristics of the transition state …

Prediction of protein-folding mechanisms from free-energy landscapes derived from native structures

E Alm, D Baker - Proceedings of the National Academy of …, 1999 - National Acad Sciences
Guided by recent experimental results suggesting that protein-folding rates and mechanisms
are determined largely by native-state topology, we develop a simple model for protein …

Topology, stability, sequence, and length: defining the determinants of two-state protein folding kinetics

KW Plaxco, KT Simons, I Ruczinski, D Baker - Biochemistry, 2000 - ACS Publications
The fastest simple, single domain proteins fold a million times more rapidly than the slowest.
Ultimately this broad kinetic spectrum is determined by the amino acid sequences that …

Protein folding is slaved to solvent motions

H Frauenfelder, PW Fenimore… - Proceedings of the …, 2006 - National Acad Sciences
Proteins, the workhorses of living systems, are constructed from chains of amino acids,
which are synthesized in the cell based on the instructions of the genetic code and then …