The Exact Nuclear Overhauser Enhancement: Recent Advances

Although often depicted as rigid structures, proteins are highly dynamic systems, whose motions are essential to their functions. Despite this, it is difficult to investigate protein dynamics due to the rapid timescale at which they sample their conformational space, leading most NMR-determined stru...

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Vydáno v:Molecules (Basel, Switzerland) Ročník 22; číslo 7; s. 1176
Hlavní autoři: Nichols, Parker, Born, Alexandra, Henen, Morkos, Strotz, Dean, Orts, Julien, Olsson, Simon, Güntert, Peter, Chi, Celestine, Vögeli, Beat
Médium: Journal Article
Jazyk:angličtina
Vydáno: Switzerland MDPI AG 14.07.2017
MDPI
Témata:
allostery
Amino Acid Sequence
biological macromolecules
conformational space
correlated dynamics
Cyclophilin A - chemistry
dynamics
exact NOE
Humans
Kinetics
Models, Molecular
Molecular Dynamics Simulation
Molecular Structure
Motion
NIMA-Interacting Peptidylprolyl Isomerase - chemistry
NMR
Nuclear Magnetic Resonance, Biomolecular - methods
Protein Conformation
Proteins
Review
structure calculation
structure ensemble
Structure-Activity Relationship
structure calculation
NMR
dynamics
structure ensemble
proteins
exact NOE
correlated dynamics
biological macromolecules
allostery
conformational space
ISSN:1420-3049, 1431-5157, 1420-3049
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Popis
Shrnutí:Although often depicted as rigid structures, proteins are highly dynamic systems, whose motions are essential to their functions. Despite this, it is difficult to investigate protein dynamics due to the rapid timescale at which they sample their conformational space, leading most NMR-determined structures to represent only an averaged snapshot of the dynamic picture. While NMR relaxation measurements can help to determine local dynamics, it is difficult to detect translational or concerted motion, and only recently have significant advances been made to make it possible to acquire a more holistic representation of the dynamics and structural landscapes of proteins. Here, we briefly revisit our most recent progress in the theory and use of exact nuclear Overhauser enhancements (eNOEs) for the calculation of structural ensembles that describe their conformational space. New developments are primarily targeted at increasing the number and improving the quality of extracted eNOE distance restraints, such that the multi-state structure calculation can be applied to proteins of higher molecular weights. We then review the implications of the exact NOE to the protein dynamics and function of cyclophilin A and the WW domain of Pin1, and finally discuss our current research and future directions.
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ISSN:1420-3049
1431-5157
1420-3049
DOI:10.3390/molecules22071176