Guzman-Luna et al. present a crosslinking analysis of the interaction of unstructured nascent chains with ribosomal proteins near the nascent polypeptide exit tunnel of the ribosome. They further analyze the dependence of these interactions on the peptide length, surface charge and ionic strength (including Mg+2 concentration), facilitating the understanding of co-translational protein folding and misfolding/aggregation
The biosynthesis of proteins occurs at the ribosomes, where amino acids are linked together into lin...
The exit tunnel of the ribosome is commonly considered to be sufficiently narrow that co-translation...
AbstractIn recent years, various folding zones within the ribosome tunnel have been identified and e...
All proteins assembled by the ribosome must pass through the nascent-peptide exit tunnel. Some nasce...
Interactions between emerging nascent polypeptide chains and the ribosome can modulate cotranslation...
Cellular proteins begin to fold as they emerge from the ribosome. The folding landscape of nascent c...
During translation, the ribosome reads the genetic code of the messenger RNA, adding one amino acid ...
The crucial molecular events accompanying protein folding in the cell are still largely unexplored. ...
Protein biosynthesis is inherently coupled to cotranslational protein folding. Folding of the nascen...
Most proteins begin to fold during biosynthesis on the ribosome. It has been suggested that interact...
As translation proceeds, the nascent polypeptide chain passes through a tunnel in the large ribosoma...
In the cell, the first time a protein has the opportunity to fold is co-translationally. In addition...
AbstractDuring protein biosynthesis, a nascent protein is exposed to multiple environments and prote...
In this report, we describe insights into the function of the ribosome tunnel that were obtained thr...
Proteins can begin the conformational search for their native structure in parallel with biosynthesi...
The biosynthesis of proteins occurs at the ribosomes, where amino acids are linked together into lin...
The exit tunnel of the ribosome is commonly considered to be sufficiently narrow that co-translation...
AbstractIn recent years, various folding zones within the ribosome tunnel have been identified and e...
All proteins assembled by the ribosome must pass through the nascent-peptide exit tunnel. Some nasce...
Interactions between emerging nascent polypeptide chains and the ribosome can modulate cotranslation...
Cellular proteins begin to fold as they emerge from the ribosome. The folding landscape of nascent c...
During translation, the ribosome reads the genetic code of the messenger RNA, adding one amino acid ...
The crucial molecular events accompanying protein folding in the cell are still largely unexplored. ...
Protein biosynthesis is inherently coupled to cotranslational protein folding. Folding of the nascen...
Most proteins begin to fold during biosynthesis on the ribosome. It has been suggested that interact...
As translation proceeds, the nascent polypeptide chain passes through a tunnel in the large ribosoma...
In the cell, the first time a protein has the opportunity to fold is co-translationally. In addition...
AbstractDuring protein biosynthesis, a nascent protein is exposed to multiple environments and prote...
In this report, we describe insights into the function of the ribosome tunnel that were obtained thr...
Proteins can begin the conformational search for their native structure in parallel with biosynthesi...
The biosynthesis of proteins occurs at the ribosomes, where amino acids are linked together into lin...
The exit tunnel of the ribosome is commonly considered to be sufficiently narrow that co-translation...
AbstractIn recent years, various folding zones within the ribosome tunnel have been identified and e...