Is polyproline II a major backbone conformation in unfolded proteins?
Z Shi, RW Woody, NR Kallenbach - Advances in protein chemistry, 2002 - Elsevier
Publisher Summary Protein folding is a process by which a polypeptide chain acquires its
native structure from an unfolded state through a transition state. Recent studies of the …
native structure from an unfolded state through a transition state. Recent studies of the …
Role of cofactors in metalloprotein folding
CJ Wilson, D Apiyo… - Quarterly reviews of …, 2004 - cambridge.org
Metals are commonly found as natural constituents of proteins. Since many such metals can
interact specifically with their corresponding unfolded proteins in vitro, cofactor-binding prior …
interact specifically with their corresponding unfolded proteins in vitro, cofactor-binding prior …
Intrinsic disorder in measles virus nucleocapsids
MR Jensen, G Communie… - Proceedings of the …, 2011 - National Acad Sciences
The genome of measles virus is encapsidated by multiple copies of the nucleoprotein (N),
forming helical nucleocapsids of molecular mass approaching 150 Megadalton. The …
forming helical nucleocapsids of molecular mass approaching 150 Megadalton. The …
Coupled prediction of protein secondary and tertiary structure
The strong coupling between secondary and tertiary structure formation in protein folding is
neglected in most structure prediction methods. In this work we investigate the extent to …
neglected in most structure prediction methods. In this work we investigate the extent to …
Thermodynamics and kinetics of non-native interactions in protein folding: a single point mutant significantly stabilizes the N-terminal domain of L9 by modulating non …
JH Cho, S Sato, DP Raleigh - Journal of molecular biology, 2004 - Elsevier
Comparatively little is known about the role of non-native interactions in protein folding and
their role in both folding and stability is controversial. We demonstrate that non-native …
their role in both folding and stability is controversial. We demonstrate that non-native …
Understanding the mechanism of β-hairpin folding via ϕ-value analysis
The folding kinetics of a 16-residue β-hairpin (trpzip4) and five mutants were studied by a
laser-induced temperature-jump infrared method. Our results indicate that mutations which …
laser-induced temperature-jump infrared method. Our results indicate that mutations which …
Energetically significant networks of coupled interactions within an unfolded protein
Unfolded and partially unfolded proteins participate in a wide range of biological processes
from pathological aggregation to the regulation of normal cellular activity. Unfolded states …
from pathological aggregation to the regulation of normal cellular activity. Unfolded states …
Tracking multiple genomic elements using correlative CRISPR imaging and sequential DNA FISH
Live imaging of genome has offered important insights into the dynamics of the genome
organization and gene expression. The demand to image simultaneously multiple genomic …
organization and gene expression. The demand to image simultaneously multiple genomic …
The denatured state of engrailed homeodomain under denaturing and native conditions
U Mayor, JG Grossmann, NW Foster… - Journal of molecular …, 2003 - Elsevier
Protein folding starts from the elusive form of the denatured state that is present under
conditions that favour the native state. We have studied the denatured state of Engrailed …
conditions that favour the native state. We have studied the denatured state of Engrailed …
Role of cofactors in folding of the blue-copper protein azurin
P Wittung-Stafshede - Inorganic chemistry, 2004 - ACS Publications
Many proteins in living cells coordinate cofactors, such as metal ions, to attain their activity.
Since the cofactors in such cases often can interact with their corresponding unfolded …
Since the cofactors in such cases often can interact with their corresponding unfolded …