NMR paper Aberrant increase of NMR signal in hydrogen exchange experiments. Observation and explanation.

		BioNMR > Educational resources > Journal club
[NMR paper] Aberrant increase of NMR signal in hydrogen exchange experiments. Observation and explanation.

Webservers

NMR processing:

MDD

NMR assignment:

Backbone:

Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

Template-based:

GeNMR

I-TASSER

Refinement:

Amber

Structure from chemical shifts:

Fragment-based:

Homology-based:

Torsion angles from chemical shifts:

Preditor

TALOS

Promega- Proline

Secondary structure from chemical shifts:

CSI (via RCI server)

TALOS

MICS caps, β-turns

d2D

PECAN

Flexibility from chemical shifts:

RCI

Interactions from chemical shifts:

HADDOCK

Chemical shifts re-referencing:

NMR model quality:

NOEs, other restraints:

Chemical shifts:

RDCs:

Pseudocontact shifts:

Protein geomtery:

SAVES2 or SAVES4

Quality Control Check

NMR spectrum prediction:

FANDAS

MestReS

V-NMR

Flexibility from structure:

Backbone S2

Methyl S2

B-factor

Molecular dynamics:

Gromacs

Amber

Antechamber

Chemical shifts prediction:

From structure:

Shiftx2

Sparta+

Camshift

CH3shift- Methyl

ArShift- Aromatic

ShiftS

Proshift

PPM

CheShift-2- Cα

From sequence:

Shifty

Camcoil

Poulsen_rc_CS

Disordered proteins:

MAXOCC

Format conversion & validation:

CCPN

From NMR-STAR 3.1

Validate NMR-STAR 3.1

NMR sample preparation:

Protein disorder:

DisMeta

Protein solubility:

Isotope labeling:

Solid-state NMR:

Thread Tools

Search this Thread

Rate Thread

Display Modes

08-22-2016, 10:38 AM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,777

Points: 193,617, Level: 100

Level up: 0%, 0 Points needed

Activity: 50.7%

Last Achievements

Award-Showcase

NMR Credits: 0

NMR Points: 193,617

Downloads: 0

Uploads: 0

Aberrant increase of NMR signal in hydrogen exchange experiments. Observation and explanation.

Aberrant increase of NMR signal in hydrogen exchange experiments. Observation and explanation.

Aberrant increase of NMR signal in hydrogen exchange experiments. Observation and explanation.

Biochem Biophys Res Commun. 2016 Aug 17;

Authors: Xue M, Kitahara R, Yoshimura Y, Mulder FA

Abstract
Hydrogen exchange (HX) NMR spectroscopy is widely used for monitoring structure, stability and dynamics of proteins at the level of individual residues. The stochastic replacement of protons by deuterons typically leads to an exponential decrease of the NMR signals. However, an unusual signal increase was observed in HX of several amides for T4 lysozyme L99A. This effect can be attributed to peak sharpening as a result of reduced dipolar relaxation from proximal amide protons that experience more rapid hydrogen/deuterium (H/D) exchange. The behavior was specifically observed at the termini of secondary structure elements, where large differences in protection against H/D exchange are observed. This effect is expected to be more widespread in NMR HX studies, and is important for the accurate determination of protection factors.

PMID: 27544032 [PubMed - as supplied by publisher]

More...

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
Selective observation of the disordered import signal of a globular protein by in-cell NMR: The example of frataxins Selective observation of the disordered import signal of a globular protein by in-cell NMR: The example of frataxins Abstract We have exploited the capability of in-cell NMR to selectively observe flexible regions within folded proteins to carry out a comparative study of two members of the highly conserved frataxin family which are found both in prokaryotes and in eukaryotes. They all contain a globular domain which shares more than 50% identity, which in eukaryotes is preceded by an N-terminal tail containing the mitochondrial import signal. We demonstrate that the NMR spectrum of...	nmrlearner	Journal club	0	04-10-2015 09:46 AM
[NMR paper] Selective observation of the disordered import signal of a globular protein by in-cell NMR: The example of frataxins. Selective observation of the disordered import signal of a globular protein by in-cell NMR: The example of frataxins. Selective observation of the disordered import signal of a globular protein by in-cell NMR: The example of frataxins. Protein Sci. 2015 Mar 12; Authors: Popovic M, Sanfelice D, Pastore C, Prischi F, Temussi PA, Pastore A Abstract We have exploited the capability of in-cell NMR to selectively observe flexible regions within folded proteins to carry out a comparative study of two members of the highly...	nmrlearner	Journal club	0	03-17-2015 05:12 PM
Selective observation of the disordered import signal of a globular protein by in-cell NMR: The example of frataxins Selective observation of the disordered import signal of a globular protein by in-cell NMR: The example of frataxins Abstract We have exploited the capability of in-cell NMR to selectively observe flexible regions within folded proteins to carry out a comparative study of two members of the highly conserved frataxin family which are found both in prokaryotes and in eukaryotes. They all contain a globular domain which shares more than 50% identity, which in eukaryotes is preceded by an N-terminal tail containing the mitochondrial import signal. We demonstrate that the NMR spectrum of the...	nmrlearner	Journal club	0	03-12-2015 11:38 PM
[NMR paper] [Interactions between proteins and cation exchange adsorbents analyzed by NMR and hydrogen/deuterium exchange technique]. . . Sheng Wu Gong Cheng Xue Bao. 2014 Sep;30(9):1454-63 Authors: Wang K, Hao D, Qi S, Ma G Abstract In silico acquirement of the accurate residue details of protein on chromatographic media is a bottleneck in protein chromatography separation and purification. Here we developed a novel approach by coupling with H/D exchange and nuclear magnetic resonance to observe hen egg white lysozyme (HEWL) unfolding behavior adsorbed on cation exchange media (SP Sepharose FF). Analysis of 1D 1H-NMR shows that protein unfolding accelerated...	nmrlearner	Journal club	0	03-01-2015 12:18 PM
Billion-fold increase in NMR signal for ions in solution Billion-fold increase in NMR signal for ions in solution http://www.spectroscopynow.com/common/images/thumbnails/14956a7fee1.jpg?-NMR spectroscopy, previously used for nuclear physics and solid-state physics, has now been applied to solutions, providing unprecedented sensitivity for magnesium ions. More...	nmrlearner	News from NMR blogs	0	10-28-2014 02:42 PM
Measuring hydrogen exchange in proteins by selective water saturation in 1Hâ??15N SOFAST/BEST-type experiments: advantages and limitations Measuring hydrogen exchange in proteins by selective water saturation in 1Hâ??15N SOFAST/BEST-type experiments: advantages and limitations Abstract HETex-SOFAST NMR (Schanda et al. in J Biomol NMR 33:199â??211, 2006) has been proposed some years ago as a fast and sensitive method for semi-quantitative measurement of site-specific amide-water hydrogen exchange effects along the backbone of proteins. Here we extend this concept to BEST readout sequences that provide a better resolution at the expense of some loss in sensitivity. We discuss the...	nmrlearner	Journal club	0	08-30-2014 11:00 PM
[NMR paper] Use of H/D isotope effects to gather information about hydrogen bonding and hydrogen exchange rates Use of H/D isotope effects to gather information about hydrogen bonding and hydrogen exchange rates Publication date: Available online 11 October 2013 Source:Journal of Magnetic Resonance</br> Author(s): Mitsuhiro Takeda , Yohei Miyanoiri , Tsutomu Terauchi , Chin-Jiun Yang , Masatsune Kainosho</br> Polar side-chains in proteins play important roles in formingand maintaining three-dimensional structures, and thus participate invarious biological functions. Until recently, most protein NMR studieshave focused onthe non-exchangeable protons of amino acid...	nmrlearner	Journal club	0	10-11-2013 10:43 AM
[NMR paper] Editing of chemical exchange-relayed NOEs in NMR experiments for the observation of p Editing of chemical exchange-relayed NOEs in NMR experiments for the observation of protein-water interactions. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Editing of chemical exchange-relayed NOEs in NMR experiments for the observation of protein-water interactions. J Magn Reson. 1999 Feb;136(2):214-8 Authors: Melacini G, Kaptein R, Boelens R An experimental approach for the editing of exchange-relayed NOEs in water-selective NOE experiments is presented. The...	nmrlearner	Journal club	0	08-21-2010 04:03 PM

« Previous Thread | Next Thread »

Posting Rules
You may not post new threads You may not post replies You may not post attachments You may not edit your posts BB code is On Smilies are On [IMG] code is On HTML code is On Trackbacks are Off Pingbacks are Off Refbacks are Off