denatured states
Recently Published Documents


TOTAL DOCUMENTS

122
(FIVE YEARS 5)

H-INDEX

36
(FIVE YEARS 2)

Life ◽  
2022 ◽  
Vol 12 (1) ◽  
pp. 123
Author(s):  
Astra Piccinini ◽  
Eva C. Lourenço ◽  
Osvaldo S. Ascenso ◽  
Maria Rita Ventura ◽  
Heinz Amenitsch ◽  
...  

Many proteins are usually not stable under different stresses, such as temperature and pH variations, mechanical stresses, high concentrations, and high saline contents, and their transport is always difficult, because they need to be maintained in a cold regime, which is costly and very challenging to achieve in remote areas of the world. For this reason, it is extremely important to find stabilizing agents that are able to preserve and protect proteins against denaturation. In the present work, we investigate, by extensively using synchrotron small-angle X-ray scattering experiments, the stabilization effect of five different sugar-derived compounds developed at ExtremoChem on two model proteins: myoglobin and insulin. The data analysis, based on a novel method that combines structural and thermodynamic features, has provided details about the physical-chemical processes that regulate the stability of these proteins in the presence of stabilizing compounds. The results clearly show that some modified sugars exert a greater stabilizing effect than others, being able to maintain the active forms of proteins at temperatures higher than those in which proteins, in the absence of stabilizers, reach denatured states.


Author(s):  
Heike Rösner ◽  
Martina Caldarini ◽  
Gregory Potel ◽  
Daniel Malmodin ◽  
Maria Vanoni ◽  
...  

The denatured state of several proteins has been shown to display transient structures that are relevant for folding, stability and aggregation. To detect them by nuclear magnetic resonance (NMR) spectroscopy, the denatured state must be stabilized by chemical agents or changes in temperature. This makes the environment different from that experienced in biologically relevant processes. Using high-resolution heteronuclear NMR spectroscopy, we have characterized several denatured states of a monomeric variant of HIV-1 protease induced by different concentrations of urea, guanidinium chloride and acetic acid. We have extrapolated the chemical shifts and the relaxation parameters to the denaturant-free denatured state at native conditions, showing that they converge to the same values. Subsequently, we characterized the conformational properties of this biologically relevant denatured state under native conditions by advanced molecular dynamics simulations and validated the results by comparison to experimental data. We show that the denatured state of HIV-1 protease under native conditions displays rich patterns of transient native and non-native structures, which could be of relevance to its guidance through a complex folding process.


2020 ◽  
Vol 11 (34) ◽  
pp. 9141-9153
Author(s):  
Georg Krainer ◽  
Andreas Hartmann ◽  
Vadim Bogatyr ◽  
Janni Nielsen ◽  
Michael Schlierf ◽  
...  

Multi-stage unfolding of S6 in SDS involving various types of denatured states with different levels of compactness and dynamics.


2019 ◽  
Vol 431 (15) ◽  
pp. 2790-2809 ◽  
Author(s):  
Yi Lei Tan ◽  
James Mitchell ◽  
Judith Klein-Seetharaman ◽  
Daniel Nietlispach

2018 ◽  
Vol 430 (21) ◽  
pp. 4068-4086 ◽  
Author(s):  
Yi Lei Tan ◽  
James Mitchell ◽  
Judith Klein-Seetharaman ◽  
Daniel Nietlispach

2018 ◽  
Vol 9 (27) ◽  
pp. 5871-5882 ◽  
Author(s):  
Shiwen Guo ◽  
Qingnan Tang ◽  
Mingxi Yao ◽  
Huijuan You ◽  
Shimin Le ◽  
...  

The differential structural–elastic properties of molecules between their transition and initial (native or denatured) states determine force-dependent transition rates.


2017 ◽  
Vol 112 (3) ◽  
pp. 57a
Author(s):  
Katherina Hemmen ◽  
Dmitro Rodnin ◽  
Igor Markovic ◽  
Thomas Otavio Peulen ◽  
Suren Felekyan ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document