Nuclear magnetic resonance (NMR) spectroscopy has made quantum leaps in the last decade, becoming a staple tool in such divergent fields as chemistry, physics, materials science, biology, and medicine. That is why it is essential that scientists working in these areas be fully conversant with current NMR theory and practice.
(BQ) Part 2 book "A complete introduction to modern NMR spectroscopy" has contents: The study of dynamic processes by NMR; electron paramagnetic resonance spectroscopy and chemically induced dynamic nuclear polarization; double resonance techniques and complex pulse sequences, two-dimensional nuclear magnetic resonance, NMR studies of biological important molecules,...and other contents.
NMR spectroscopy is a powerful tool for studying the structure, function
and dynamics of biological macromolecules. However, non-spectroscopists
often find NMR theory daunting and data interpretation nontrivial. As the
first of two back-to-back reviews on NMR spectroscopy aimed at non-spectroscopists
uclear magnetic resonance spectroscopy can now be used to investigate the biochemical energetics of human tissues and organs noninvasively. The method already has increased our understanding of some muscle diseases, has provided information from muscle metabolism about whole-body functions, control, and hormonal status, has helped in the elucidation of hitherto unrecognized causes of disease, and yielded new ideas about the control of bioenergetics in vivo. Studies on the biochemistry of human brain, liver, heart, and kidney are just beginning.
This book has evolved from over a quarter-century of research that concentrated on
delineating the aqueous coordination reactions that characterize the vanadium(V)
oxidation state. At the beginning of this time period, only a minor amount of research
was being done on vanadium aqueous chemistry. However, the basic tenets of
NMR spectroscopy were being elaborated, and some of the influences of ligand
properties and coordination geometry on the NMR spectra were being ascertained.
Lecture Organic chemistry - Chapter 10: Nuclear magnetic resonance (NMR) spectroscopy. In this chapter, the following content will be discussed: What is spectroscopy? General spectrometer, the chemical shift δ, complex splitting patterns,...and other contents.
Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học General Psychiatry cung cấp cho các bạn kiến thức về ngành y đề tài: Localized 1H-NMR spectroscopy in patients with fibromyalgia: a controlled study of changes in cerebral glutamate/glutamine, inositol, choline, and N-acetylaspartate...
A strength of NMR spectroscopy is its ability to monitor, on an atomic
level, molecular changes and interactions. In this review, which is intended
for non-spectroscopists, we describe major uses of NMR in protein science
beyond solution structure determination.
We have isolated a nonfucosylated and three variously
fucosylated neutral oligosaccharides from human milk that
are based on theiso-lacto-N-octaose core. Their structures
were characterized by the combined use of electrospray
mass spectrometry (ES-MS) and NMR spectroscopy. The
branching pattern and blood group-related Lewis deter-minants, together with partial sequences and linkages of
these oligosaccharides, were initially elucidated by high-sensitivity ES-MS/MS analysis, and then their full structure
assignment was completed by methylation analysis and
Cell-free protein synthesis offers rapidaccess toproteins that
are selectively labelledwith [
N]aminoacids andsuitable for
analysis by NMR spectroscopy without chromatographic
purification. A system based on anEscherichia colicell ex-tractwas optimizedwith regard toproteinyieldandminimal
N-labelled amino acid, and examined for the
presence of metabolic by-products which could interfere
with the NMR analysis. Yields of up to 1.8 mg of human
cyclophilin A per mL of reactionmedium were obtained by
expression of a synthetic gene. ...
Human serum albumin (HSA) is best known for its extraordinary ligand
binding capacity. HSA has a high affinity for heme and is responsible for
the transport of medium and long chain fatty acids. Here, we report myri-state binding to the N and B conformational states of Mn(III)heme–HSA
(i.e. at pH 7.0 and 10.0, respectively) as investigated by optical absorbance
and NMR spectroscopy. At pH 7.0, Mn(III)heme binds to HSA with lower
affinity than Fe(III)heme, and displays a water molecule coordinated to the
Cellulose and wheat straw degradation byRuminococcus albuswas moni-tored using NMR spectroscopy. In situ solid-state
magic angle spinning NMR was used to monitor the modification of the
composition and structure of cellulose and
C-enriched wheat straw during
the growth of the bacterium on these substrates.
Recent research has established NMR as a key method for high-through-put comparative analysis of plant extracts. We discuss recent examples of
the use of NMR to provide metabolomic data for various applications in
plant science and look forward to the key role that NMR will play in data
provision for plant systems biology.
The 3D structure of a complex formed by the acidic fibroblast growth fac-tor (FGF-1) and a specifically designed synthetic heparin hexasaccharide
has been determined by NMR spectroscopy. This hexasaccharide can sub-stitute natural heparins in FGF-1 mitogenesis assays, in spite of not indu-cing any apparent dimerization of the growth factor.
Using solution NMR spectroscopy, three-dimensional structures have been
obtained for an 18-residue synthetic polypeptide fragment of 18.5 kDa
myelin basic protein (MBP, human residues Q81–T98) under three condi-tions emulating the protein’s natural environment in the myelin membrane
to varying degrees: (a) an aqueous solution (100 mmKCl pH 6.5), (b) a
mixture of trifluoroethanol (TFE-d2) and water (30 : 70% v⁄v), and (c) a
dispersion of 100 mm dodecylphosphocholine (DPC-d38
, 1 : 100 pro-tein⁄lipid molar ratio) micelles....
The coat proteins of filamentous phage are first synthesized as transmem-brane proteins and then assembled onto the extruding viral particles. We
investigated the transmembrane conformation of the Pseudomonas aerugi-nosa Pf3 phage coat protein using proton-decoupled
solid-state NMR spectroscopy.
Thioredoxin reductase (TrxR) fromEscherichia coli,the
mutant proteins E159Y and C138S, and the mutant
protein C138Streated with phenylmercuric acetate were
reconstituted with [U-13
N4]FAD and analysed, in
their oxidized and reduced states, by
P-NMR spectroscopy. The enzymes studied showed
P-NMR spectra in the oxidized state, con-sisting of two peaks at )9.8 and )11.5 p.p.m. In the
reduced state, the two peaks merge into one apparent
peak (at)9.8 p.p.m.)....
Leukocytes and other cells show an enhanced intensity of
mobile lipid in their
H NMR spectra under a variety of
conditions.Such conditions include stimulation, which has
recently been shown to involve detergent-resistant, plasma
membranedomains (DRMs)oftencalled lipidrafts.As there
ismuchspeculationsurrounding theoriginof cellularNMR-visible lipid, we analysed subcellular fractions, including
DRMs, by NMR spectroscopy.