Example of Journal of Biomolecular Structure and Dynamics format
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Example of Journal of Biomolecular Structure and Dynamics format Example of Journal of Biomolecular Structure and Dynamics format Example of Journal of Biomolecular Structure and Dynamics format Example of Journal of Biomolecular Structure and Dynamics format Example of Journal of Biomolecular Structure and Dynamics format Example of Journal of Biomolecular Structure and Dynamics format Example of Journal of Biomolecular Structure and Dynamics format Example of Journal of Biomolecular Structure and Dynamics format Example of Journal of Biomolecular Structure and Dynamics format Example of Journal of Biomolecular Structure and Dynamics format Example of Journal of Biomolecular Structure and Dynamics format Example of Journal of Biomolecular Structure and Dynamics format Example of Journal of Biomolecular Structure and Dynamics format Example of Journal of Biomolecular Structure and Dynamics format Example of Journal of Biomolecular Structure and Dynamics format Example of Journal of Biomolecular Structure and Dynamics format Example of Journal of Biomolecular Structure and Dynamics format Example of Journal of Biomolecular Structure and Dynamics format Example of Journal of Biomolecular Structure and Dynamics format Example of Journal of Biomolecular Structure and Dynamics format Example of Journal of Biomolecular Structure and Dynamics format Example of Journal of Biomolecular Structure and Dynamics format Example of Journal of Biomolecular Structure and Dynamics format Example of Journal of Biomolecular Structure and Dynamics format
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open access Open Access

Journal of Biomolecular Structure and Dynamics — Template for authors

Publisher: Taylor and Francis
Categories Rank Trend in last 3 yrs
Molecular Biology #197 of 382 down down by 2 ranks
Structural Biology #26 of 48 down down by 5 ranks
journal-quality-icon Journal quality:
Medium
calendar-icon Last 4 years overview: 1302 Published Papers | 6552 Citations
indexed-in-icon Indexed in: Scopus
last-updated-icon Last updated: 17/07/2020
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Related Journals

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Springer

Quality:  
High
CiteRatio: 9.6
SJR: 1.766
SNIP: 1.645
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Elsevier

Quality:  
High
CiteRatio: 8.5
SJR: 3.189
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Elsevier

Quality:  
High
CiteRatio: 9.0
SJR: 2.907
SNIP: 1.268
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Elsevier

Quality:  
High
CiteRatio: 12.4
SJR: 3.935
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Journal Performance & Insights

CiteRatio

SCImago Journal Rank (SJR)

Source Normalized Impact per Paper (SNIP)

A measure of average citations received per peer-reviewed paper published in the journal.

Measures weighted citations received by the journal. Citation weighting depends on the categories and prestige of the citing journal.

Measures actual citations received relative to citations expected for the journal's category.

5.0

11% from 2019

CiteRatio for Journal of Biomolecular Structure and Dynamics from 2016 - 2020
Year Value
2020 5.0
2019 4.5
2018 4.7
2017 4.4
2016 3.8
graph view Graph view
table view Table view

0.448

11% from 2019

SJR for Journal of Biomolecular Structure and Dynamics from 2016 - 2020
Year Value
2020 0.448
2019 0.504
2018 0.718
2017 0.654
2016 0.698
graph view Graph view
table view Table view

0.987

1% from 2019

SNIP for Journal of Biomolecular Structure and Dynamics from 2016 - 2020
Year Value
2020 0.987
2019 0.98
2018 0.811
2017 0.847
2016 0.79
graph view Graph view
table view Table view

insights Insights

  • CiteRatio of this journal has increased by 11% in last years.
  • This journal’s CiteRatio is in the top 10 percentile category.

insights Insights

  • SJR of this journal has decreased by 11% in last years.
  • This journal’s SJR is in the top 10 percentile category.

insights Insights

  • SNIP of this journal has increased by 1% in last years.
  • This journal’s SNIP is in the top 10 percentile category.

Journal of Biomolecular Structure and Dynamics

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Taylor and Francis

Journal of Biomolecular Structure and Dynamics

The Journal of Biomolecular Structure and Dynamics welcomes manuscripts on biological structure, dynamics, interactions and expression. The Journal is one of the leading publications in high end computational science, atomic structural biology, bioinformatics, virtual drug des...... Read More

Medicine

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Last updated on
17 Jul 2020
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ISSN
0739-1102
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Acceptance Rate
Not Provided
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Frequency
Not Provided
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Open Access
Not Provided
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Sherpa RoMEO Archiving Policy
Green faq
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Plagiarism Check
Available via Turnitin
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Endnote Style
Download Available
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Bibliography Name
Taylor and Francis Custom Citation
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Citation Type
Numbered
[25]
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Bibliography Example
Blonder GE, Tinkham M, Klapwijk TM. Transition from metallic to tunneling regimes in superconducting microconstrictions: Excess current, charge imbalance, and supercurrent conversion. Phys Rev B. 1982; 25(7):4515–4532. Available from: 10.1103/PhysRevB.25.4515.

Top papers written in this journal

Journal Article DOI: 10.1080/07391102.1999.10508297
A modified version of the Cornell et al. force field with improved sugar pucker phases and helical repeat.
Thomas E. Cheatham1, Piotr Cieplak2, Peter A. Kollman3

Abstract:

We have examined some subtle parameter modifications to the Cornell et al. force field, which has proven quite successful in reproducing nucleic acid properties, but whose C2'-endo sugar pucker phase and helical repeat for B DNA appear to be somewhat underestimated. Encouragingly, the addition of a single V2 term involving th... We have examined some subtle parameter modifications to the Cornell et al. force field, which has proven quite successful in reproducing nucleic acid properties, but whose C2'-endo sugar pucker phase and helical repeat for B DNA appear to be somewhat underestimated. Encouragingly, the addition of a single V2 term involving the atoms C(sp3)-O-(sp3)-C(sp3)-N(sp2), which can be nicely rationalized because of the anomeric effect (lone pairs on oxygen are preferentially oriented relative to the electron withdrawing N), brings the sugar pucker phase of C2'-endo sugars to near perfect agreement with ab initio calculations (W near 162 degrees). Secondly, the use of high level ab initio calculations on entire nucleosides (in contrast to smaller model systems necessitated in 1994-95 by computer limitations) lets one improve the chi torsional potential for nucleic acids. Finally, the O(sp3)-C(sp3)- C(sp3)-O(sp3) V2 torsional potential has been empirically adjusted to reproduce the ab initio calculated relative energy of C2'-endo and C3'-endo nucleosides. These modifications are tested in molecular dynamics simulations of mononucleosides (to assess sugar pucker percentages) and double helices of DNA and RNA (to assess helical and sequence specific structural properties). In both areas, the modified force field leads to improved agreement with experimental data. read more read less

Topics:

Ab initio (55%)55% related to the paper, Ab initio quantum chemistry methods (50%)50% related to the paper
915 Citations
Journal Article DOI: 10.1080/07391102.1988.10506483
The Definition of Generalized Helicoidal Parameters and of Axis Curvature for Irregular Nucleic Acids

Abstract:

An algorithm is presented which solves the problem of obtaining a rigorous helicoidal description of an irregular nucleic acid segment. Central to this approach is the definition of a function describing simultaneously the curvature of the nucleic acid segment in question and the corresponding stepwise variation of helicoidal... An algorithm is presented which solves the problem of obtaining a rigorous helicoidal description of an irregular nucleic acid segment. Central to this approach is the definition of a function describing simultaneously the curvature of the nucleic acid segment in question and the corresponding stepwise variation of helicoidal parameters along the segment. Minimisation of this function leads to an optimal distribution of the conformational irregularity of the segment between these two components. Further, it is shown that this approach can be applied equally easily to single or double stranded nucleic acids. The results of this analysis yield both the absolute helicoidal parameters of individual bases/base pairs and the relative helicoidal parameters between successive bases/base pairs as well as the overall locus of the helical axis. The possibilities of this mathematical approach are demonstrated with the help of a computer program termed "Curves" which is applied to the study of a number of different nucleic acid structures. read more read less
885 Citations
Journal Article DOI: 10.1080/07391102.1989.10507728
Defining the structure of irregular nucleic acids: conventions and principles.

Abstract:

The algorithm "Curves", that we have recently presented in this journal (J. Biolmol. Str. Dynam. 6, 63-91 (1988], is updated to take into account the conventions developed at the Cambridge meeting on DNA curvature (September 1988) and extended to the calculation of local parameters. In addition, the principles which govern th... The algorithm "Curves", that we have recently presented in this journal (J. Biolmol. Str. Dynam. 6, 63-91 (1988], is updated to take into account the conventions developed at the Cambridge meeting on DNA curvature (September 1988) and extended to the calculation of local parameters. In addition, the principles which govern the choices made in establishing the Curves algorithm are compared with the approaches adopted by other authors. read more read less
687 Citations
Journal Article DOI: 10.1080/07391102.2003.10506918
A Protein-Chameleon: Conformational Plasticity of α-Synuclein, a Disordered Protein Involved in Neurodegenerative Disorders
Vladimir N. Uversky1

Abstract:

Under the physiological conditions in vitro, α-synuclein, a conservative presynaptic protein, the aggregation and fibrillation of which is assumed to be involved into the pathogenesis of Parkinson's disease and several other neurodegenerative disorders, known as synucleinopathies, is characterized by the lack of rigid well-de... Under the physiological conditions in vitro, α-synuclein, a conservative presynaptic protein, the aggregation and fibrillation of which is assumed to be involved into the pathogenesis of Parkinson's disease and several other neurodegenerative disorders, known as synucleinopathies, is characterized by the lack of rigid well-defined structure; i.e., it belongs to the class of intrinsically unstructured proteins. Intriguingly, α-synuclein is characterized by a remarkable conformational plasticity, adopting a series of different conformations depending on the environment. For example, this protein may either stay substantially unfolded, or adopt an amyloidogenic partially folded conformation, or fold into α-helical or β-structural species, both monomeric and oligomeric. Furthermore, it might form several morphologically different types of aggregates, including oligomers (spheres or doughnuts), amorphous aggregates, and or amyloid-like fibrils. The peculiarities of this astonishing conformational beha... read more read less

Topics:

Protein structure (55%)55% related to the paper, Alpha-synuclein (53%)53% related to the paper, Protein folding (53%)53% related to the paper, Synucleinopathies (53%)53% related to the paper
477 Citations
Journal Article DOI: 10.1080/07391102.2012.675145
Orderly order in protein intrinsic disorder distribution: disorder in 3500 proteomes from viruses and the three domains of life
Bin Xue1, A. Keith Dunker2, Vladimir N. Uversky2

Abstract:

Intrinsically disordered proteins and intrinsically disordered protein regions are highly abundant in nature. However, the quantitative and qualitative measures of protein intrinsic disorder in species with known genomes are still not available. Furthermore, although the correlation between high fraction of disordered residue... Intrinsically disordered proteins and intrinsically disordered protein regions are highly abundant in nature. However, the quantitative and qualitative measures of protein intrinsic disorder in species with known genomes are still not available. Furthermore, although the correlation between high fraction of disordered residues and advanced species has been reported, the details of this correlation and the connection between the disorder content and proteome complexity have not been reported as of yet. To fill this gap, we analysed entire proteomes of 3484 species from three domains of life (archaea, bacteria and eukaryotes) and from viruses. Our analysis revealed that the evolution process is characterized by distinctive patterns of changes in the protein intrinsic disorder content. We are showing here that viruses are characterized by the widest spread of the proteome disorder content (the percentage of disordered residues ranges from 7.3% in human coronavirus NL63 to 77.3% in Avian carcinoma virus). For several organisms, a clear correlation is seen between their disorder contents and habitats. In multicellular eukaryotes, there is a weak correlation between the complexity of an organism (evaluated as a number of different cell types) and its overall disorder content. For both the prokaryotes and eukaryotes, the disorder content is generally independent of the proteome size. However, disorder shows a sharp increase associated with the transition from prokaryotic to eukaryotic cells. This suggests that the increased disorder content in eukaryotic proteomes might be used by nature to deal with the increased cell complexity due to the appearance of the various cellular compartments. read more read less

Topics:

Proteome (55%)55% related to the paper, Intrinsically disordered proteins (54%)54% related to the paper
472 Citations
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Frequently asked questions

1. Can I write Journal of Biomolecular Structure and Dynamics in LaTeX?

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2. Do you follow the Journal of Biomolecular Structure and Dynamics guidelines?

Yes, the template is compliant with the Journal of Biomolecular Structure and Dynamics guidelines. Our experts at SciSpace ensure that. If there are any changes to the journal's guidelines, we'll change our algorithm accordingly.

3. Can I cite my article in multiple styles in Journal of Biomolecular Structure and Dynamics?

Of course! We support all the top citation styles, such as APA style, MLA style, Vancouver style, Harvard style, and Chicago style. For example, when you write your paper and hit autoformat, our system will automatically update your article as per the Journal of Biomolecular Structure and Dynamics citation style.

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12. Is Journal of Biomolecular Structure and Dynamics's impact factor high enough that I should try publishing my article there?

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13. What is Sherpa RoMEO Archiving Policy for Journal of Biomolecular Structure and Dynamics?

SHERPA/RoMEO Database

We extracted this data from Sherpa Romeo to help researchers understand the access level of this journal in accordance with the Sherpa Romeo Archiving Policy for Journal of Biomolecular Structure and Dynamics. The table below indicates the level of access a journal has as per Sherpa Romeo's archiving policy.

RoMEO Colour Archiving policy
Green Can archive pre-print and post-print or publisher's version/PDF
Blue Can archive post-print (ie final draft post-refereeing) or publisher's version/PDF
Yellow Can archive pre-print (ie pre-refereeing)
White Archiving not formally supported
FYI:
  1. Pre-prints as being the version of the paper before peer review and
  2. Post-prints as being the version of the paper after peer-review, with revisions having been made.

14. What are the most common citation types In Journal of Biomolecular Structure and Dynamics?

The 5 most common citation types in order of usage for Journal of Biomolecular Structure and Dynamics are:.

S. No. Citation Style Type
1. Author Year
2. Numbered
3. Numbered (Superscripted)
4. Author Year (Cited Pages)
5. Footnote

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16. Can I download Journal of Biomolecular Structure and Dynamics in Endnote format?

Yes, SciSpace provides this functionality. After signing up, you would need to import your existing references from Word or Bib file to SciSpace. Then SciSpace would allow you to download your references in Journal of Biomolecular Structure and Dynamics Endnote style according to Elsevier guidelines.

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