Protein folding is a fundamental biological process of great significance for cell function and
life-related processes. Surprisingly, very little is presently known about how proteins fold in …

The relation between co-and post-translational protein folding and aggregation in the cell is
poorly understood. Here, we employ a combination of fluorescence anisotropy decays in the …

Anfinsen's thermodynamic hypothesis does not explicitly take into account the possibility of
protein aggregation. Here, we introduce a cyclic-perturbation approach to prove that not only …

In order to elucidate the relative importance of secondary structure and topology in
determining folding mechanism, we have carried out a phi-value analysis of the death …

Photochemically induced dynamic nuclear polarization (photo-CIDNP) of nuclei other than
1H offers a tremendous potential for sensitivity enhancement in liquid state NMR under mild …

In order to become bioactive, proteins must be translated and protected from aggregation
during biosynthesis. The ribosome and molecular chaperones play a key role in this …

Heme ligation in hemoglobin is typically assumed by the “proximal” histidine. Hydrophobic
contacts, ionic interactions, and the ligation bond secure the heme between two α-helices …

Photochemically induced dynamic nuclear polarization (photo-CIDNP) is usually employed
as a probe of solvent exposure in biomolecular NMR. The potential of the photo-CIDNP …

The growing interest in protein folding under physiologically relevant conditions has
prompted investigations requiring direct comparisons between ribosome-bound and …

Myoglobins are ubiquitous proteins that play a seminal role in oxygen storage, transport,
and NO metabolism. The folding mechanism of apomyoglobins from different species has …