Intrinsically disordered protein
Proteins can exist in a trinity of structures: the ordered state, the molten globule, and the
random coil. The five following examples suggest that native protein structure can …
random coil. The five following examples suggest that native protein structure can …
The application of circular dichroism to studies of protein folding and unfolding
SM Kelly, NC Price - Biochimica et Biophysica Acta (BBA)-Protein Structure …, 1997 - Elsevier
In this review, we shall outline the basic principles Ž. of circular dichroism CD and indicate
the types of structural information relevant to the study of the Ž. folding and unfolding or …
the types of structural information relevant to the study of the Ž. folding and unfolding or …
Role of the molten globule state in protein folding
M Arai, K Kuwajima - Advances in protein chemistry, 2000 - Elsevier
Publisher Summary This chapter deals with the structure of the molten globules of various
globular proteins revealed by the recent experimental studies. Recent advances in …
globular proteins revealed by the recent experimental studies. Recent advances in …
Protein folding intermediates and pathways studied by hydrogen exchange
SW Englander - Annual review of biophysics and biomolecular …, 2000 - annualreviews.org
▪ Abstract In order to solve the immensely difficult protein-folding problem, it will be
necessary to characterize the barriers that slow folding and the intermediate structures that …
necessary to characterize the barriers that slow folding and the intermediate structures that …
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 …
Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding
The structure and dynamics of two partially folded states of apomyoglobin have been
characterized at equilibrium using multi-dimensional NMR spectroscopy. Residue-specific …
characterized at equilibrium using multi-dimensional NMR spectroscopy. Residue-specific …
Direct observation of fast protein folding: the initial collapse of apomyoglobin.
RM Ballew, J Sabelko… - Proceedings of the …, 1996 - National Acad Sciences
The rapid refolding dynamics of apomyoglobin are followed by a new temperature-jump
fluorescence technique on a 15-ns to 0.5-ms time scale in vitro. The apparatus measures the …
fluorescence technique on a 15-ns to 0.5-ms time scale in vitro. The apparatus measures the …
Protein folding and misfolding: mechanism and principles
SW Englander, L Mayne, MMG Krishna - Quarterly reviews of …, 2007 - cambridge.org
Two fundamentally different views of how proteins fold are now being debated. Do proteins
fold through multiple unpredictable routes directed only by the energetically downhill nature …
fold through multiple unpredictable routes directed only by the energetically downhill nature …
A residue-specific NMR view of the non-cooperative unfolding of a molten globule
Molten globules are partially folded forms of proteins that are thought to be general
intermediates in protein folding. Nonetheless, there is limited structural information about …
intermediates in protein folding. Nonetheless, there is limited structural information about …
The hydrogen exchange core and protein folding
R Li, C Woodward - Protein Science, 1999 - cambridge.org
A database of hydrogen-deuterium exchange results has been compiled for proteins for
which there are published rates of out-exchange in the native state, protection against …
which there are published rates of out-exchange in the native state, protection against …