Journal of Biomolecular Nmr
Overview
The Journal of Biomolecular NMR is a peer-reviewed scientific journal that focuses on the field of nuclear magnetic resonance (NMR) spectroscopy applied to the study of biological macromolecules. It publishes high-quality research articles, reviews, and technical notes, covering topics such as protein structure determination, ligand-receptor interactions, and dynamics of biomolecular systems. The journal serves as a valuable resource for researchers and practitioners in the field of biomolecular NMR, providing insights into the structure, function, and dynamics of biological molecules at the a
Details
Details
Abbr.
J Biomol NMR
Publisher
Springer
Start
1991
End
Continuing
Frequency
12 no. a year, 1999-
p-ISSN
0925-2738
e-ISSN
1573-5001
Country
Netherlands
Language
English
Specialties
Molecular Biology
Nuclear Medicine
Nuclear Medicine
Metrics
Metrics
h-index / Ranks: 2493
113
SJR / Ranks: 5111
817
CiteScore / Ranks: 3060
6.80
JIF / Ranks: 3958
2.7
Recent Articles
1.
Saberi M, Dekkers R, Passerini L, Huber M, Overhand M, Ubbink M
J Biomol NMR
. 2025 Mar;
PMID: 40072774
Paramagnetic probes provide long-range distance information and report on minor conformations of biomacromolecules. However, it is important to realize that any probe can affect the system of interest. Here, we...
2.
ODea F, Seargeant A, Hurcum J, do Aido-Machado R, Rowe M, Baxter N, et al.
J Biomol NMR
. 2025 Mar;
PMID: 40063318
Addition of glycine betaine up to 1 M gave rise to increased intensity for some weak signals in the HSQC spectra of barnase and Plasmodium falciparum flap endonuclease. The signals...
3.
Dag C, Kahraman K
J Biomol NMR
. 2025 Mar;
PMID: 40048033
The use of Escherichia coli for recombinant protein production is a cornerstone in structural biology, particularly for nuclear magnetic resonance (NMR) spectroscopy studies. Understanding the metabolic behavior of E. coli...
4.
Trevino M
J Biomol NMR
. 2025 Mar;
PMID: 40024995
NMR is a powerful tool for the structural and dynamic study of proteins. One of the necessary conditions for the study of these proteins is their isotopic labelling with N...
5.
Braun D, Kauffmann C, Beier A, Ceccolini I, Lebedenko O, Skrynnikov N, et al.
J Biomol NMR
. 2025 Feb;
PMID: 40011319
Structurally diverse ensembles of intrinsically disordered proteins or regions are difficult to determine, because experimental observables usually report a conformational average. Therefore, in order to infer the underlying distribution, a...
6.
Picard L, Pichugin D, Huang S, Suleiman M, Prosser R
J Biomol NMR
. 2025 Feb;
PMID: 39960596
Large proteins and dilute spin systems within a deuterated background are often characterized by long proton (H) spin-lattice relaxation times (T), which directly impacts the recycle delay and hence, the...
7.
Gopinath T, Kraft A, Shin K, Wood N, Marassi F
J Biomol NMR
. 2025 Jan;
79(1):35-45.
PMID: 39881117
The NMR signals from protein sidechains are rich in information about intra- and inter-molecular interactions, but their detection can be complicated due to spectral overlap as well as conformational and...
8.
Oster C, Chevelkov V, Lange A
J Biomol NMR
. 2025 Jan;
79(1):25-34.
PMID: 39841396
Chemical shift assignments of large membrane proteins by solid-state NMR experiments are challenging. Recent advancements in sensitivity-enhanced pulse sequences, have made it feasible to acquire H-detected 4D spectra of these...
9.
Rodella M, Schneider R, Kummerle R, Felli I, Pierattelli R
J Biomol NMR
. 2025 Jan;
79(1):15-24.
PMID: 39841395
Intrinsically disordered proteins and protein regions are central to many biological processes but difficult to characterize at atomic resolution. Nuclear magnetic resonance is particularly well-suited for providing structural and dynamical...
10.
Shen Y, Smith M, Louis J, Bax A
J Biomol NMR
. 2024 Dec;
79(1):47-57.
PMID: 39661299
Inclusion of residual dipolar couplings (RDCs) during the early rounds of protein structure determination requires use of a floating alignment tensor or knowledge of the alignment tensor strength and rhombicity....