Identification of a Collapsed Intermediate with Non-native Long-range Interactions on the Folding Pathway of a Pair of Fyn SH3 Domain Mutants by NMR Relaxation Dispersion Spectroscopy

2006 ◽  
Vol 363 (5) ◽  
pp. 958-976 ◽  
Author(s):  
Philipp Neudecker ◽  
Arash Zarrine-Afsar ◽  
Wing-Yiu Choy ◽  
D. Ranjith Muhandiram ◽  
Alan R. Davidson ◽  
...  
Keyword(s):  
Long Range ◽  
Nmr Relaxation ◽  
Sh3 Domain ◽  
Relaxation Dispersion ◽  
Folding Pathway ◽  
Long Range Interactions

scholarly journals Nonnative Interactions in the FF Domain Folding Pathway from an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study

2011 ◽  
Vol 133 (28) ◽  
pp. 10974-10982 ◽  
Author(s):  
Dmitry M. Korzhnev ◽  
Robert M. Vernon ◽  
Tomasz L. Religa ◽  
Alexandar L. Hansen ◽  
David Baker ◽  
...  
Keyword(s):  
Nmr Relaxation ◽  
Relaxation Dispersion ◽  
Atomic Resolution ◽  
Folding Pathway ◽  
Resolution Structure

Multiple-Site Exchange in Proteins Studied with a Suite of Six NMR Relaxation Dispersion Experiments:  An Application to the Folding of a Fyn SH3 Domain Mutant

2005 ◽  
Vol 127 (44) ◽  
pp. 15602-15611 ◽  
Author(s):  
Dmitry M. Korzhnev ◽  
Philipp Neudecker ◽  
Anthony Mittermaier ◽  
Vladislav Yu. Orekhov ◽  
Lewis E. Kay
Keyword(s):  
Nmr Relaxation ◽  
Sh3 Domain ◽  
Relaxation Dispersion ◽  
Multiple Site ◽  
Site Exchange

scholarly journals Structural Changes in the Acceptor Site of Photosystem II upon Ca2+/Sr2+ Exchange in the Mn4CaO5 Cluster Site and the Possible Long-Range Interactions

Biomolecules ◽  
2019 ◽  
Vol 9 (8) ◽  
pp. 371
Author(s):  
Koua
Keyword(s):  
Crystal Structure ◽  
Photosystem Ii ◽  
Long Range ◽  
Electron Acceptor ◽  
Structural Changes ◽  
Acceptor Site ◽  
Oxygen Evolving Complex ◽  
Long Range Interactions ◽  
Structural Perturbations ◽  
Oxygen Evolving

The Mn4CaO5 cluster site in the oxygen-evolving complex (OEC) of photosystem II (PSII) undergoes structural perturbations, such as those induced by Ca2+/Sr2+ exchanges or Ca/Mn removal. These changes have been known to induce long-range positive shifts (between +30 and +150 mV) in the redox potential of the primary quinone electron acceptor plastoquinone A (QA), which is located 40 Å from the OEC. To further investigate these effects, we reanalyzed the crystal structure of Sr-PSII resolved at 2.1 Å and compared it with the native Ca-PSII resolved at 1.9 Å. Here, we focus on the acceptor site and report the possible long-range interactions between the donor, Mn4Ca(Sr)O5 cluster, and acceptor sites.

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