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verified SJR 0,652 · Q2 • database Scopus / SJR & Web of Science indexed
Journal of Biomolecular NMR
Netherlands · Springer Science and Busines...
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Journal of Biomolecular NMR

Journal of Biomolecular NMR is a journal indexed in SJR in Biochemistry and Spectroscopy with an H index of 114. It has a price of 2590 €. It has an SJR impact factor of 0,652 and it has a best quartile of Q2. It is published in English. It has an SJR impact factor of 0,652.

ISSN: 0925-2738
Publisher: Springer Science and Business Media B.V.
Category: Biochemistry
Indexation: verifiedScopus / SJR verifiedWeb of Science
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schedule CountryOfPapers database fields
SJR Impact Factor trending_up
0,652 Q2
H-index 114
Acceptance rate pie_chart
24% Selective
Source Acceptance_Rate
Time to publication hourglass_top
NPD
Field NPD
Publication cost (APC) payments
2.590 € Open Access
Non-OA path 0 €

Metrics

Scimago and CountryOfPapers database fields

Scopus / SJR Web of Science

SJR Impact

0,652

H-index

114

Docs (year)

24

Docs 3y

73

Total refs

1109

Cites 3y

160

Citable 3y

72

Cites/Doc 2y

2.1

Ref/Doc

46.21

Immediate OA

2590 €

Embargoed OA

NPD

Non OA / Submission

0 €

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Best articles by citations

Combined frequency- and time-domain NMR spectroscopy. Application to fast protein resonance assignment

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Using codon optimization, chaperone co-expression, and rational mutagenesis for production and NMR assignments of human eIF2a

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Letter to the Editor: Assignment of the1H,13C, and15N resonances of the AXH domain of the transcription factor HBP1

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Letter to the Editor: Assignment of the1H,13C and15N Resonances of the LpxC Deacetylase from Aquifex aeolicus in Complex with the Substrate-Analog Inhibitor TU-514

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Letter to the Editor: Assignment of the1H,13C and15N resonances of the catalytic domain of guanine nucleotide exchange factor BopE from Burkholderia pseudomallei

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Interpretation of NMR relaxation properties of Pin1, a two-domain protein, based on Brownian dynamic simulations

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Improving the Accuracy of NMR Structures of Large Proteins Using Pseudocontact Shifts as Long-Range Restraints

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Improvement of hydrogen bond geometry in protein NMR structures by residual dipolar couplings -an assessment of the interrelation of NMR restraints

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Heteronuclear 2D (1H-13C) MAS NMR Resolves the Electronic Structure of Coordinated Histidines in Light-Harvesting Complex II: Assessment of Charge Transfer and Electronic Delocalization Effect

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Fast reconstruction of four-dimensional NMR spectra from plane projections

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Exploring signal-to-noise ratio and sensitivity in non-uniformly sampled multi-dimensional NMR spectra

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Erratum: Paramagnetism-based restraints for Xplor-NIH

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SHOW MORE ARTICLES

Erratum: Application of correlated residual dipolar couplings to the determination of the molecular alignment tensor magnitude of oriented proteins and nucleic acids

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A complete set of novel 2D correlation NMR experiments based on heteronuclear J-cross polarization

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Characterization of threonine side chain dynamics in an antifreeze protein using natural abundance13C NMR spectroscopy

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Carbonyl carbon transverse relaxation dispersion measurements and ms-µs timescale motion in a protein hydrogen bond network

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Binding ability of a HHP-tagged protein towards Ni2+studied by paramagnetic NMR relaxation: The possibility of obtaining long-range structure information

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BACUS: A Bayesian protocol for the identification of protein NOESY spectra via unassigned spin systems*

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Assignment validation software suite for the evaluation and presentation of protein resonance assignment data

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Assignment of protein backbone resonances using connectivity, torsion angles and13Cachemical shifts

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Application of Correlated Residual Dipolar Couplings to the Determination of the Molecular Alignment Tensor Magnitude of Oriented Proteins and Nucleic Acids

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Application of 1D and 2D NMR techniques to the structure elucidation of the O-polysaccharide from Proteus mirabilis O: 57

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An expectation/maximization nuclear vector replacement algorithm for automated NMR resonance assignments

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Adiabatic TOBSY in rotating solids

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