Many small, monomeric proteins fold with simple two-state kinetics and show wide variation in folding rates, from microseconds to seconds. Thus, stable intermediates are not a prerequisite for the fast, efficient folding of proteins and may in fact be kinetic traps and slow the folding process. Using recent studies, can we begin to search for trends which may lead to a better understanding of the protein folding process
Tesis doctoral inédita leída en la Universidad Autónoma de Madrid, Facultad de Ciencias, Departament...
The fastest simple, kinetically two-state protein folds a million times more rapidly than the slowes...
Over the past three decades the protein folding field has undergone monumental changes. Originally a...
AbstractUnderstanding how proteins fold is one of the central problems in biochemistry. A new genera...
10 pages, 7 figures.-- PMID: 16834320 [PubMed].-- PMCID: PMC2546509.-- Author manuscript available i...
For many decades, protein folding experimentalists have worked with no information about the timesca...
AbstractA major question about protein folding is whether the coming together by diffusion of differ...
Backgound:The role of intermediates in protein folding has been a matter of great controversy. Altho...
Abstract. This thesis describes factors that are rate limiting for the folding of two small proteins...
Although intermediates have long been recognised as fascinating species that form during the folding...
BackgroundRecent data have suggested two principles that are central to the work we describe here. F...
AbstractExperimentally measured rates of spontaneous folding of single-domain globular proteins rang...
Systematic studies of kinetics using minimal protein models reveal multiple folding nuclei for seque...
Backgound:The role of intermediates in protein folding has been a matter of great controversy. Altho...
AbstractThermodynamic measurements of proteins indicate that the folding to the native state takes p...
Tesis doctoral inédita leída en la Universidad Autónoma de Madrid, Facultad de Ciencias, Departament...
The fastest simple, kinetically two-state protein folds a million times more rapidly than the slowes...
Over the past three decades the protein folding field has undergone monumental changes. Originally a...
AbstractUnderstanding how proteins fold is one of the central problems in biochemistry. A new genera...
10 pages, 7 figures.-- PMID: 16834320 [PubMed].-- PMCID: PMC2546509.-- Author manuscript available i...
For many decades, protein folding experimentalists have worked with no information about the timesca...
AbstractA major question about protein folding is whether the coming together by diffusion of differ...
Backgound:The role of intermediates in protein folding has been a matter of great controversy. Altho...
Abstract. This thesis describes factors that are rate limiting for the folding of two small proteins...
Although intermediates have long been recognised as fascinating species that form during the folding...
BackgroundRecent data have suggested two principles that are central to the work we describe here. F...
AbstractExperimentally measured rates of spontaneous folding of single-domain globular proteins rang...
Systematic studies of kinetics using minimal protein models reveal multiple folding nuclei for seque...
Backgound:The role of intermediates in protein folding has been a matter of great controversy. Altho...
AbstractThermodynamic measurements of proteins indicate that the folding to the native state takes p...
Tesis doctoral inédita leída en la Universidad Autónoma de Madrid, Facultad de Ciencias, Departament...
The fastest simple, kinetically two-state protein folds a million times more rapidly than the slowes...
Over the past three decades the protein folding field has undergone monumental changes. Originally a...