"Invisible" Conformers of an Antifungal Disulfide Protein Revealed by Constrained Cold and Heat Unfolding, CEST-NMR Experiments, and Molecular Dynamics Calculations.

Transition between conformational states in proteins is being recognized as a possible key factor of function. In support of this, hidden dynamic NMR structures were detected in several cases up to populations of a few percent. Here, we show by two- and three-state analysis of thermal unfolding,...

Full description

Bibliographic Details
Main Authors: Fizil Ádám
Gáspári Zoltán
Barna Teréz
Marx F
Batta Gyula
Format: Article
Published: 2015
Series:CHEMISTRY-A EUROPEAN JOURNAL 21 No. 13
Subjects:
Kémiai tudományok
mtmt:2871042
Online Access:https://publikacio.ppke.hu/1469

MARC

LEADER 00000nab a2200000 i 4500
001 publ1469
005 20241024141801.0
008 241024s2015 hu o 0|| Angol d
022 |a 0947-6539 
024 7 |a 2871042  |2 mtmt 
040 |a PPKE Publikáció Repozitórium  |b hun 
041 |a Angol 
100 1 |a Fizil Ádám 
245 1 0 |a "Invisible" Conformers of an Antifungal Disulfide Protein Revealed by Constrained Cold and Heat Unfolding, CEST-NMR Experiments, and Molecular Dynamics Calculations.  |h [elektronikus dokumentum] /  |c  Fizil Ádám 
260 |c 2015 
300 |a 5136-5144 
490 0 |a CHEMISTRY-A EUROPEAN JOURNAL  |v 21 No. 13 
520 3 |a Transition between conformational states in proteins is being recognized as a possible key factor of function. In support of this, hidden dynamic NMR structures were detected in several cases up to populations of a few percent. Here, we show by two- and three-state analysis of thermal unfolding, that the population of hidden states may weight 20-40 % at 298 K in a disulfide-rich protein. In addition, sensitive (15) N-CEST NMR experiments identified a low populated (0.15 %) state that was in slow exchange with the folded PAF protein. Remarkably, other techniques failed to identify the rest of the NMR "dark matter". Comparison of the temperature dependence of chemical shifts from experiments and molecular dynamics calculations suggests that hidden conformers of PAF differ in the loop and terminal regions and are most similar in the evolutionary conserved core. Our observations point to the existence of a complex conformational landscape with multiple conformational states in dynamic equilibrium, with diverse exchange rates presumably responsible for the completely hidden nature of a considerable fraction. 
650 4 |a Kémiai tudományok 
700 0 1 |a Gáspári Zoltán  |e aut 
700 0 1 |a Barna Teréz  |e aut 
700 0 1 |a Marx F  |e aut 
700 0 1 |a Batta Gyula  |e aut 
856 4 0 |u https://publikacio.ppke.hu/id/eprint/1469/1/ChemistryAEuropeanJ-2015-Fizil-InvisibleConformersofanAntifungalDisulfideProteinRevealedbyConstrained.pdf  |z Dokumentum-elérés  

Similar Items