An ultrafast laser temperature jump (T-jump) induces folding and unfolding of Wh5 (see picture), the shortest possible α-helical peptide. Using time-resolved fluorescence spectroscopy, the folding time of this peptide was found to span from less than one nanosecond to a few nanoseconds, redefining the meaning of ultrafast dynamics in protein and peptide folding
Determining the rate of forming the truly folded conformation of ultrafast folding proteins is an im...
Understanding the folding of the β-hairpin is a crucial step in studying how β-rich proteins fold. W...
As the simplest and most prevalent motif of protein folding, α-helix initiation is the starting poin...
An ultrafast laser temperature jump (T-jump) induces folding and unfolding of Wh5 (see picture), the...
The dynamics of protein folding has become a major area of research interest today, particularly in ...
Using time-resolved IR spectroscopy, we monitored the kinetics of folding and unfolding processes of...
Experimental techniques have now reached the sub-microsecond timescale necessary to study fast event...
The importance of protein folding simply stems from the fact that proteins assume well-defined three...
The understanding of fast folding dynamics of single α-helices comes mostly from studies on rational...
The small size (58 residues) and simple structure of the B domain of staphylococcal protein A (BdpA)...
A protein’s folding and conformational energy landscape depends on a large number of molecular degre...
A protein’s folding and conformational energy landscape depends on a large number of molecular degre...
The time-scales of protein folding events range over many orders of magnitude. In order to understan...
AbstractThe thermal unfolding of a series of 6-, 10-, and 14-mer cyclic β-hairpin peptides was studi...
International audienceThe use of a fast temperature jump (T-jump) is a very powerful experiment aimi...
Determining the rate of forming the truly folded conformation of ultrafast folding proteins is an im...
Understanding the folding of the β-hairpin is a crucial step in studying how β-rich proteins fold. W...
As the simplest and most prevalent motif of protein folding, α-helix initiation is the starting poin...
An ultrafast laser temperature jump (T-jump) induces folding and unfolding of Wh5 (see picture), the...
The dynamics of protein folding has become a major area of research interest today, particularly in ...
Using time-resolved IR spectroscopy, we monitored the kinetics of folding and unfolding processes of...
Experimental techniques have now reached the sub-microsecond timescale necessary to study fast event...
The importance of protein folding simply stems from the fact that proteins assume well-defined three...
The understanding of fast folding dynamics of single α-helices comes mostly from studies on rational...
The small size (58 residues) and simple structure of the B domain of staphylococcal protein A (BdpA)...
A protein’s folding and conformational energy landscape depends on a large number of molecular degre...
A protein’s folding and conformational energy landscape depends on a large number of molecular degre...
The time-scales of protein folding events range over many orders of magnitude. In order to understan...
AbstractThe thermal unfolding of a series of 6-, 10-, and 14-mer cyclic β-hairpin peptides was studi...
International audienceThe use of a fast temperature jump (T-jump) is a very powerful experiment aimi...
Determining the rate of forming the truly folded conformation of ultrafast folding proteins is an im...
Understanding the folding of the β-hairpin is a crucial step in studying how β-rich proteins fold. W...
As the simplest and most prevalent motif of protein folding, α-helix initiation is the starting poin...