Folding mechanism of the C‐terminal domain of nucleophosmin: residual structure in the denatured state and its pathophysiological significance

2009 ◽  
Vol 23 (8) ◽  
pp. 2360-2365 ◽  
Author(s):  
Flavio Scaloni ◽  
Stefano Gianni ◽  
Luca Federici ◽  
Brunangelo Falini ◽  
Maurizio Brunori
Keyword(s):  
Denatured State ◽  
Residual Structure ◽  
Folding Mechanism ◽  
Terminal Domain

scholarly journals Structural dissection of alkaline-denatured pepsin

2004 ◽  
Vol 18 (2) ◽  
pp. 227-236 ◽  
Author(s):  
Yuji O. Kamatari ◽  
Christopher M. Dobson ◽  
Takashi Konno
Keyword(s):  
Limited Proteolysis ◽  
Helical Structure ◽  
Cd Spectroscopy ◽  
Core Region ◽  
Detailed Knowledge ◽  
Native State ◽  
Denatured State ◽  
Residual Structure ◽  
Alkaline Denaturation ◽  
Folded Core

Pepsin, a gastric aspartic proteinase, is a zymogen‒derived protein that undergoes irreversible alkaline denaturation at pH 6–7. Detailed knowledge of the structure of the alkaline‒denatured state is an important step in understanding the mechanism of the formation of the active enzyme. It has been established in a number of studies that the alkaline‒denatured state of pepsin (the IPstate) is composed of a compact C‒terminal lobe and a largely unstructured N‒terminal lobe. In the present study, we have investigated the residual structure in the IPstate in more detail, using limited proteolysis to isolate and characterize a tightly folded core region from this partially denatured pepsin. The isolated core region corresponds to the 141 C‒terminal residues of the pepsin molecule, which in the fully native state forms one of the two lobes of the structure. A comparative study using NMR and CD spectroscopy has revealed, however, that the N‒terminal lobe contributes a substantial amount of additional residual structure to the IPstate of pepsin. CD spectra indicate in addition that significant non‒native α-helical structure is present in the C‒terminal lobe of the structure when the N‒terminal lobe of pepsin is either unfolded or removed by proteolysis. This study demonstrates that the structure of pepsin in the IPstate is significantly more complex than that of a fully folded C‒terminal lobe connected to an unstructured N‒terminal lobe. The “misfolding” in this state could inhibit the proper refolding of the protein when returned to conditions that stabilize the native state.

The Denatured States of Lysozyme

1973 ◽  
Vol 51 (5) ◽  
pp. 581-585 ◽  
Author(s):  
M. Kugimiya ◽  
C. C. Bigelow
Keyword(s):  
Lithium Perchlorate ◽  
Difference Spectroscopy ◽  
Hen Egg White Lysozyme ◽  
Guanidinium Chloride ◽  
Denatured State ◽  
Residual Structure ◽  
Egg White Lysozyme ◽  
Temperature State ◽  
Hen Egg White ◽  
Denatured States

The denaturation of hen egg-white lysozyme has been studied under a variety of denaturing conditions by difference spectroscopy, polarimetry, and viscometry. It has been found that the lysozyme molecule can take up four different denatured conformations, depending on the denaturant used. Urea and guanidinium chloride produce the most completely denatured state, IV, and, listed in the order of increasing residual structure, lithium chloride gives state III, temperature state II, and lithium perchlorate state I. Differences in the spectra at 300 nm have been a valuable aid in relating the different denatured states to each other.

scholarly journals The Cold Denatured State of the C-terminal Domain of Protein L9 Is Compact and Contains Both Native and Non-native Structure

2010 ◽  
Vol 132 (13) ◽  
pp. 4669-4677 ◽  
Author(s):  
Bing Shan ◽  
Sebastian McClendon ◽  
Carla Rospigliosi ◽  
David Eliezer ◽  
Daniel P. Raleigh
Keyword(s):  
Native Structure ◽  
Denatured State ◽  
Terminal Domain

scholarly journals Irreversible Thermal Denaturation of Glucose Oxidase fromAspergillus nigerIs the Transition to the Denatured State with Residual Structure

2004 ◽  
Vol 279 (46) ◽  
pp. 47601-47609 ◽  
Author(s):  
Gabriel Zoldák ◽  
Anton Zubrik ◽  
Andrej Musatov ◽  
Marek Stupák ◽  
Erik Sedlák
Keyword(s):  
Glucose Oxidase ◽  
Thermal Denaturation ◽  
Denatured State ◽  
Residual Structure
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