scholarly journals Hydrogen bond strength in membrane proteins probed by time-resolved 1 H-detected solid-state NMR and MD simulations

2017 ◽  
Vol 87 ◽  
pp. 80-85 ◽  
Author(s):  
João Medeiros-Silva ◽  
Shehrazade Jekhmane ◽  
Marc Baldus ◽  
Markus Weingarth
Keyword(s):  
Hydrogen Bond ◽  
Solid State ◽  
Membrane Proteins ◽  
Bond Strength ◽  
Solid State Nmr ◽  
Md Simulations ◽  
Time Resolved ◽  
Hydrogen Bond Strength

Refinement of hydrogen atomic position in a hydrogen bond using a combination of solid-state NMR and computation

2003 ◽  
pp. 2834 ◽  
Author(s):  
Robin K. Harris ◽  
Phuong Y. Ghi ◽  
Robert B. Hammond ◽  
Cai-Yun Ma ◽  
Kevin J. Roberts
Keyword(s):  
Hydrogen Bond ◽  
Solid State ◽  
Solid State Nmr ◽  
Atomic Position

Solid state NMR of membrane proteins: methods and applications

2021 ◽  
Author(s):  
Vivien Yeh ◽  
Boyan B. Bonev
Keyword(s):  
Solid State ◽  
High Resolution ◽  
Membrane Proteins ◽  
Solid State Nmr ◽  
Lipid Membrane ◽  
Cell Function ◽  
Membrane Lipid ◽  
Pharmacological Intervention ◽  
Nmr Methods ◽  
Informative Approach

Membranes of cells are active barriers, in which membrane proteins perform essential remodelling, transport and recognition functions that are vital to cells. Membrane proteins are key regulatory components of cells and represent essential targets for the modulation of cell function and pharmacological intervention. However, novel folds, low molarity and the need for lipid membrane support present serious challenges to the characterisation of their structure and interactions. We describe the use of solid state NMR as a versatile and informative approach for membrane and membrane protein studies, which uniquely provides information on structure, interactions and dynamics of membrane proteins. High resolution approaches are discussed in conjunction with applications of NMR methods to studies of membrane lipid and protein structure and interactions. Signal enhancement in high resolution NMR spectra through DNP is discussed as a tool for whole cell and interaction studies.

Redshift or Adduct Stabilization—A Computational Study of Hydrogen Bonding in Adducts of Protonated Carboxylic Acids

2009 ◽  
Vol 15 (2) ◽  
pp. 239-248 ◽  
Author(s):  
Solveig Gaarn Olesen ◽  
Steen Hammerum
Keyword(s):  
Hydrogen Bond ◽  
Hydrogen Bonds ◽  
Bond Strength ◽  
Bond Length ◽  
Carboxylic Acids ◽  
Computational Study ◽  
Proton Affinities ◽  
Oh Groups ◽  
Hydrogen Bond Strength ◽  
Length Changes

It is generally expected that the hydrogen bond strength in a D–H•••A adduct is predicted by the difference between the proton affinities (Δ PA) of D and A, measured by the adduct stabilization, and demonstrated by the infrared (IR) redshift of the D–H bond stretching vibrational frequency. These criteria do not always yield consistent predictions, as illustrated by the hydrogen bonds formed by the E and Z OH groups of protonated carboxylic acids. The Δ PA and the stabilization of a series of hydrogen bonded adducts indicate that the E OH group forms the stronger hydrogen bonds, whereas the bond length changes and the redshift favor the Z OH group, matching the results of NBO and AIM calculations. This reflects that the thermochemistry of adduct formation is not a good measure of the hydrogen bond strength in charged adducts, and that the ionic interactions in the E and Z adducts of protonated carboxylic acids are different. The OH bond length and IR redshift afford the better measure of hydrogen bond strength.

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