netics igan the f kineti with molecules are particularly well suited for investigating the other hand, rapid folding is associated with the existence of a folding rates in a set of 24 non-homologous single domain otherwise; N is the total number of contacts and L is the protein chain length. The empirical observation that the CO correlates well with the folding rates of single domain dscapes, strongly Biophysical Chemistry 115 (2smooth, funnel-shaped energy landscape [5]. In [6,7], Plaxcocorrelations between folding times and the native state equilibrium properties, a major challenge for those working in protein research. The energy landscape theory predicts that the landscape’s ruggedness plays a fundamental role in the folding kinetics of...
The relative folding rates of simple, single-domain proteins, proteins whose folding energy landscap...
Computational studies of proteins have significantly improved our understanding of protein folding. ...
10 pages, 7 figures.-- PMID: 16834320 [PubMed].-- PMCID: PMC2546509.-- Author manuscript available i...
AbstractUnderstanding how proteins fold is one of the central problems in biochemistry. A new genera...
AbstractThe rapid folding of certain proteins can be described theoretically using an energy landsca...
AbstractA theoretical framework is developed to study the dynamics of protein folding. The key insig...
For many decades, protein folding experimentalists have worked with no information about the timesca...
We explore the correlation between the energy landscape and topology in the folding of a model prote...
By exploring the folding pathways of the B1 domain of protein L with a series of equilibrium and rap...
Protein folding is modeled as diffusion on a free-energy landscape, allowing use of the diffusion eq...
BackgroundRecent data have suggested two principles that are central to the work we describe here. F...
BackgroundRecent experimental and theoretical studies have revealed that protein folding kinetics ca...
The Notch ankyrin domain is a repeat protein whose folding has been characterized through equilibriu...
Monte Carlo simulations of a simple lattice model of protein folding show two distinct regimes depen...
The energy landscape approach has played a fundamental role in advancing our understanding of protei...
The relative folding rates of simple, single-domain proteins, proteins whose folding energy landscap...
Computational studies of proteins have significantly improved our understanding of protein folding. ...
10 pages, 7 figures.-- PMID: 16834320 [PubMed].-- PMCID: PMC2546509.-- Author manuscript available i...
AbstractUnderstanding how proteins fold is one of the central problems in biochemistry. A new genera...
AbstractThe rapid folding of certain proteins can be described theoretically using an energy landsca...
AbstractA theoretical framework is developed to study the dynamics of protein folding. The key insig...
For many decades, protein folding experimentalists have worked with no information about the timesca...
We explore the correlation between the energy landscape and topology in the folding of a model prote...
By exploring the folding pathways of the B1 domain of protein L with a series of equilibrium and rap...
Protein folding is modeled as diffusion on a free-energy landscape, allowing use of the diffusion eq...
BackgroundRecent data have suggested two principles that are central to the work we describe here. F...
BackgroundRecent experimental and theoretical studies have revealed that protein folding kinetics ca...
The Notch ankyrin domain is a repeat protein whose folding has been characterized through equilibriu...
Monte Carlo simulations of a simple lattice model of protein folding show two distinct regimes depen...
The energy landscape approach has played a fundamental role in advancing our understanding of protei...
The relative folding rates of simple, single-domain proteins, proteins whose folding energy landscap...
Computational studies of proteins have significantly improved our understanding of protein folding. ...
10 pages, 7 figures.-- PMID: 16834320 [PubMed].-- PMCID: PMC2546509.-- Author manuscript available i...