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[NMR paper] Impact of chemotherapy on metabolic reprogramming: Characterization of the metabolic profile of breast cancer MDA-MB-231 cells using (1)H HR-MAS NMR spectroscopy.
Sep 16, 2017 - 9:58 PM - by nmrlearner
nmrlearner's Avatar Impact of chemotherapy on metabolic reprogramming: Characterization of the metabolic profile of breast cancer MDA-MB-231 cells using (1)H HR-MAS NMR spectroscopy.

Related Articles Impact of chemotherapy on metabolic reprogramming: Characterization of the metabolic profile of breast cancer MDA-MB-231 cells using (1)H HR-MAS NMR spectroscopy.

J Pharm Biomed Anal. 2017 Sep 12;146:324-328

Authors: Maria RM, Altei WF, Selistre-de-Araujo HS, Colnago LA

Abstract
Doxorubicin, cisplatin, and tamoxifen are part of many chemotherapeutic regimens. However, studies investigating the effect of chemotherapy on the metabolism of breast cancer cells are still limited. We used (1)H high-resolution magic angle spinning (HR-MAS) NMR spectroscopy to study the metabolic profile of human breast cancer MDA-MB-231 cells either untreated (control) or treated with tamoxifen, cisplatin, and doxorubicin. (1)H HR-MAS NMR single pulse spectra evidenced signals from all mobile cell compounds, including fatty acids (membranes), water-soluble proteins, and metabolites. NMR spectra showed that phosphocholine (i.e., a biomarker of breast cancer malignant transformation) signals were stronger in control than in treated cells, but significantly decreased upon treatment with tamoxifen/cisplatin. NMR spectra acquired with Carr-Purcell-Meiboom-Gill (CPMG) pulse sequence were interpreted only qualitatively because signal areas were... [Read More]
0 Replies | 32 Views
[NMR paper] Cell-free protein synthesis enhancement from real-time NMR metabolite kinetics: redirecting energy fluxes in hybrid RRL systems.
Sep 16, 2017 - 9:58 PM - by nmrlearner
nmrlearner's Avatar Cell-free protein synthesis enhancement from real-time NMR metabolite kinetics: redirecting energy fluxes in hybrid RRL systems.

Related Articles Cell-free protein synthesis enhancement from real-time NMR metabolite kinetics: redirecting energy fluxes in hybrid RRL systems.

ACS Synth Biol. 2017 Sep 15;:

Authors: Panthu B, Ohlmann T, Perrier J, Schlattner U, Jalinot P, Elena-Herrmann B, Rautureau GJP

Abstract
A counter-intuitive cell-free protein synthesis (CFPS) strategy, based on reducing the ribosomal fraction in rabbit reticulocyte lysate (RRL), triggers the development of hybrid systems composed of RRL ribosome-free supernatant complemented with ribosomes from different mammalian cell-types. Hybrid RRL systems maintain translational properties of the original ribosome cell types, and deliver protein expression levels similar to RRL. Here, we show that persistent ribosome-associated metabolic activity consuming ATP is a major obstacle for maximal protein yield. We provide a detailed picture of hybrid CFPS systems energetic metabolism based on real-time nuclear magnetic resonance (NMR) investigation of metabolites kinetics. We demonstrate that protein synthesis capacity is ceiled at native ribosome concentration and that lower amounts of ribosomal fraction optimize energy fluxes toward protein translation, consequently increasing CFPS yield. These results provide a rationalized strategy... [Read More]
0 Replies | 28 Views
[NMR paper] NMR reveals the intrinsically disordered domain 2 of NS5A protein as an allosteric regulator of the hepatitis C virus RNA polymerase NS5B.
Sep 16, 2017 - 9:58 PM - by nmrlearner
nmrlearner's Avatar NMR reveals the intrinsically disordered domain 2 of NS5A protein as an allosteric regulator of the hepatitis C virus RNA polymerase NS5B.

Related Articles NMR reveals the intrinsically disordered domain 2 of NS5A protein as an allosteric regulator of the hepatitis C virus RNA polymerase NS5B.

J Biol Chem. 2017 Sep 14;:

Authors: Bessa LM, Launay H, Dujardin M, Cantrelle FX, Lippens G, Landrieu I, Schneider R, Hanoulle X

Abstract
Non-structural protein 5B (NS5B) is the RNAdependent RNA polymerase that catalyses replication of the hepatitis C virus (HCV) RNA genome, and so is central for its life cycle. NS5B interacts with the intrinsically disordered domain 2 of NS5A (NS5A-D2), another essential multifunctional HCV protein that is required for RNA replication. As a result, these two proteins represent important targets for anti-HCV chemotherapies. Despite this importance and the existence of NS5B crystal structures, our understanding of the conformational and dynamic behaviour of NS5B in solution and its relationship with NS5A-D2 remain incomplete. To address these points, we report the first detailed NMR spectroscopic study of HCV NS5B lacking its membrane anchor (NS5B?21). Analysis of constructs with selective isotope labelling of the ?1 methyl groups of isoleucine side chains demonstrates that, in solution, NS5B?21 is highly dynamic, but predominantly adopts a closed conformation.... [Read More]
0 Replies | 75 Views
[NMR paper] Direct NMR Probing of Hydration Shells of Protein Ligand Interfaces and its Application to Drug Design.
Sep 15, 2017 - 8:41 PM - by nmrlearner
nmrlearner's Avatar Direct NMR Probing of Hydration Shells of Protein Ligand Interfaces and its Application to Drug Design.

Related Articles Direct NMR Probing of Hydration Shells of Protein Ligand Interfaces and its Application to Drug Design.

J Med Chem. 2017 Sep 14;:

Authors: Geist L, Mayer M, Cockcroft XL, Wolkerstorfer B, Kessler D, Engelhardt H, McConnell DB, Konrat R

Abstract
Fragment-based drug design exploits initial screening of low molecular weight compounds and their concomitant affinity improvement. The multitude of possible chemical modifications highlights the necessity to obtain structural information about the binding mode of a fragment. Herein we describe a novel NMR methodology - LOGSY-titration - that allows the determination of binding modes of low affinity binders in the protein-ligand interface and reveals suitable ligand positions for the addition of functional groups that either address or substitute protein-bound water - information of utmost importance for drug design. The particular benefit of the methodology and in contrast to conventional ligand-based methods is the independence of the molecular weight of the protein under study. The validity of the novel approach is demonstrated on two ligands interacting with Bromodomain 1 of Bromodomain containing protein 4, a prominent cancer target in pharmaceutical industry.


PMID: 28910100 [PubMed - as supplied by... [Read More]
0 Replies | 38 Views
[NMR paper] Concepts and Methods of Solid-State NMR Spectroscopy Applied to Biomembranes.
Sep 15, 2017 - 8:41 PM - by nmrlearner
nmrlearner's Avatar Concepts and Methods of Solid-State NMR Spectroscopy Applied to Biomembranes.

Related Articles Concepts and Methods of Solid-State NMR Spectroscopy Applied to Biomembranes.

Chem Rev. 2017 Sep 14;:

Authors: Molugu TR, Lee S, Brown MF

Abstract
Concepts of solid-state NMR spectroscopy and applications to fluid membranes are reviewed in this paper. Membrane lipids with (2)H-labeled acyl chains or polar head groups are studied using (2)H NMR to yield knowledge of their atomistic structures in relation to equilibrium properties. This review demonstrates the principles and applications of solid-state NMR by unifying dipolar and quadrupolar interactions and highlights the unique features offered by solid-state (2)H NMR with experimental illustrations. For randomly oriented multilamellar lipids or aligned membranes, solid-state (2)H NMR enables direct measurement of residual quadrupolar couplings (RQCs) due to individual C-(2)H-labeled segments. The distribution of RQC values gives nearly complete profiles of the segmental order parameters SCD((i)) as a function of acyl segment position (i). Alternatively, one can measure residual dipolar couplings (RDCs) for natural abundance lipid samples to obtain segmental SCH order parameters. A theoretical mean-torque model provides acyl-packing profiles representing the cumulative chain extension along the normal to the aqueous interface. Equilibrium... [Read More]
0 Replies | 33 Views
[NMR paper] The thermodynamic basis of the fuzzy interaction of an intrinsically disordered protein
Sep 15, 2017 - 8:41 PM - by nmrlearner
nmrlearner's Avatar The thermodynamic basis of the fuzzy interaction of an intrinsically disordered protein


Many intrinsically disordered proteins (IDP) that fold upon binding retain conformational heterogeneity in IDP-target complexes. The thermodynamics of such fuzzy interactions is poorly understood. Here we introduce a thermodynamic framework, based on analysis of ITC and CD spectroscopy data, that provides experimental description of IDP association in terms of folding and binding contributions which can be predicted using sequence folding propensities and molecular modeling. We show how IDP can modulate the entropy and enthalpy by adapting their bound-state structural ensemble to achieve optimal binding. This is explained in terms of a free energy landscape that provides the relationship between free energy, sequence folding propensity and disorder. The observed "fuzzy" behavior is possible not only because of IDP flexibility but also because backbone and side chain interactions are, to some extent, energetically decoupled allowing IDP to minimize energetically unfavorable folding.

More...
0 Replies | 32 Views
Using NMR and MD simulation to study helicity in IDPs - News-Medical.net
Sep 15, 2017 - 2:17 AM - by nmrlearner
nmrlearner's Avatar
News-Medical.net


Using NMR and MD simulation to study helicity in IDPs
News-Medical.net
Particularly when combined with techniques such as nuclear magnetic resonance (NMR) spectroscopy, these studies allow atomistic understanding of the various conformations proteins adopt. One of the main techniques for modeling proteins is molecular ...

and more »

Using NMR and MD simulation... [Read More]
0 Replies | 64 Views
[NMR] Nobel Prize winner Nico Bloembergen passed away at age 97
Sep 15, 2017 - 2:17 AM - by nmrlearner
nmrlearner's Avatar From The DNP-NMR Blog:

[NMR] Nobel Prize winner Nico Bloembergen passed away at age 97



From the Ampere Magnetic Resonance List:


Dear colleagues,


Last week, Nobel laureate Professor Nicolaas Bloembergen, a pioneer in the field of NMR and laser spectroscopy passed away at age of 97. As an undergraduate Bloembergen studied Physics at Utrecht University from 1938 to 1943 and received his PhD in Physics from Leiden University with C.J. Gorter in 1948 on the topic of Nuclear Magnetic Relaxation. His thesis resulted in the famous BPP (Bloembergen, Purcell and Pound) paper which still serves as a point of departure for understanding many NMR relaxation experiments. In 1973 he returned to Leiden and occupied the Lorentz Chair in Physics. In 1981, he was awarded the Nobel Prize in Physics for his work in coherent optics. In 2001 in honour of his achievements, the NMR group at Utrecht University named their laboratory the Bloembergen Building.


For further information on a true scientific giant, please look out for an obituary written by C. Luchinat, R. Boelens, and R. Kaptein that will appear on the Ampere website and in the Ampere newsletter soon.


Also, please see, for example:
https://www.uu.nl/en/news/uu-alumnus...en-passed-away
... [Read More]
0 Replies | 45 Views
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