Example of Biochemistry format
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Example of Biochemistry format Example of Biochemistry format Example of Biochemistry format Example of Biochemistry format Example of Biochemistry format Example of Biochemistry format Example of Biochemistry format Example of Biochemistry format Example of Biochemistry format
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Example of Biochemistry format Example of Biochemistry format Example of Biochemistry format Example of Biochemistry format Example of Biochemistry format Example of Biochemistry format Example of Biochemistry format Example of Biochemistry format Example of Biochemistry format
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Biochemistry — Template for authors

Categories Rank Trend in last 3 yrs
Biochemistry #158 of 415 down down by 30 ranks
journal-quality-icon Journal quality:
Good
calendar-icon Last 4 years overview: 2311 Published Papers | 12753 Citations
indexed-in-icon Indexed in: Scopus
last-updated-icon Last updated: 13/06/2020
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Related Journals

open access Open Access
recommended Recommended

Taylor and Francis

Quality:  
High
CiteRatio: 13.9
SJR: 4.634
SNIP: 2.046
open access Open Access

Springer

Quality:  
High
CiteRatio: 4.3
SJR: 0.633
SNIP: 1.433
open access Open Access

De Gruyter

Quality:  
High
CiteRatio: 6.5
SJR: 1.246
SNIP: 0.854

Royal Society of Chemistry

Quality:  
High
CiteRatio: 6.0
SJR: 0.923
SNIP: 0.776

Journal Performance & Insights

Impact Factor

CiteRatio

Determines the importance of a journal by taking a measure of frequency with which the average article in a journal has been cited in a particular year.

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

2.865

3% from 2018

Impact factor for Biochemistry from 2016 - 2019
Year Value
2019 2.865
2018 2.952
2017 2.997
2016 2.938
graph view Graph view
table view Table view

5.5

4% from 2019

CiteRatio for Biochemistry from 2016 - 2020
Year Value
2020 5.5
2019 5.3
2018 5.2
2017 5.4
2016 5.5
graph view Graph view
table view Table view

insights Insights

  • Impact factor of this journal has decreased by 3% in last year.
  • This journal’s impact factor is in the top 10 percentile category.

insights Insights

  • CiteRatio of this journal has increased by 4% in last years.
  • This journal’s CiteRatio is in the top 10 percentile category.

SCImago Journal Rank (SJR)

Source Normalized Impact per Paper (SNIP)

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.

1.43

2% from 2019

SJR for Biochemistry from 2016 - 2020
Year Value
2020 1.43
2019 1.464
2018 1.556
2017 1.685
2016 1.737
graph view Graph view
table view Table view

0.803

1% from 2019

SNIP for Biochemistry from 2016 - 2020
Year Value
2020 0.803
2019 0.811
2018 0.844
2017 0.86
2016 0.851
graph view Graph view
table view Table view

insights Insights

  • SJR of this journal has decreased by 2% in last years.
  • This journal’s SJR is in the top 10 percentile category.

insights Insights

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

Biochemistry

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American Chemical Society

Biochemistry

The purpose of Biochemistry is to publish the results of original research that contribute significantly to the understanding of the mechanism of biological phenomena in terms of molecular structure and/or function. Submission of manuscripts in emerging areas in chemical biolo...... Read More

Biochemistry

Biochemistry, Genetics and Molecular Biology

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Last updated on
13 Jun 2020
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ISSN
0006-2960
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Impact Factor
Medium - 0.974
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Open Access
Yes
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Sherpa RoMEO Archiving Policy
Blue faq
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Plagiarism Check
Available via Turnitin
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Endnote Style
Download Available
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Bibliography Name
ACS Custom Citation (achemso)
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Citation Type
Numbered (Superscripted)
25
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Bibliography Example
Beenakker, C. W. J. Specular Andreev Reflection in Graphene. Phys. Rev. Lett. 2006, 97, 067007.

Top papers written in this journal

Journal Article DOI: 10.1021/BI00591A005
Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease.
Chirgwin John Mitchell1, Alan Przybyla2, Raymond J. MacDonald, William J. Rutter3
27 Nov 1979 - Biochemistry

Abstract:

Intact ribonucleic acid (RNA) has been prepared from tissues rich in ribonuclease such as the rat pancreas by efficient homogenization in a 4 M solution of the potent protein denaturant guanidinium thiocyanate plus 0.1 M 2-mercaptoethanol to break protein disulfide bonds. The RNA was isolated free of protein by ethanol precip... Intact ribonucleic acid (RNA) has been prepared from tissues rich in ribonuclease such as the rat pancreas by efficient homogenization in a 4 M solution of the potent protein denaturant guanidinium thiocyanate plus 0.1 M 2-mercaptoethanol to break protein disulfide bonds. The RNA was isolated free of protein by ethanol precipitation or by sedimentation through cesium chloride. Rat pancreas RNA obtained by these means has been used as a source for the purification of alpha-amylase messenger ribonucleic acid. read more read less

Topics:

Guanidinium thiocyanate (58%)58% related to the paper, Acid guanidinium thiocyanate-phenol-chloroform extraction (58%)58% related to the paper, RNA (56%)56% related to the paper, Ribonuclease (55%)55% related to the paper, Protein biosynthesis (53%)53% related to the paper
19,805 Citations
Journal Article DOI: 10.1021/BI00789A030
Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane.
22 Jun 1971 - Biochemistry

Topics:

Spectrin binding (55%)55% related to the paper
8,245 Citations
Journal Article DOI: 10.1021/BI00514A017
Thermodynamics of protein association reactions: forces contributing to stability
26 May 1981 - Biochemistry

Abstract:

Reviewing the thermodynamic parameters characterizing self-association and ligand binding of proteins at 25 OC, we find AGO, AHo, AS\", and ACpo are often all of negative sign. It is thus not possible to account for the stability of association complexes of proteins on the basis of hydrophobic interactions alone. We present a... Reviewing the thermodynamic parameters characterizing self-association and ligand binding of proteins at 25 OC, we find AGO, AHo, AS\", and ACpo are often all of negative sign. It is thus not possible to account for the stability of association complexes of proteins on the basis of hydrophobic interactions alone. We present a conceptual model of protein association consisting of two steps: the mutual penetration of hydration layers causing disordering of the solvent followed by further short-range interactions. The net AGO for the complete association process is primarily determined by the positive entropy change accompanying the first step and the negative enthalpy change of the second step. On the basis of the thermochemical behavior of small molecule interactions, we conclude that the strengthening of hydrogen bonds in the I n the past decade, a complete thermodynamic description of the self-association of many proteins and their interactions From the Laboratory of Molecular Biology (P.D.R.) and Laboratory of Nutrition and Endocrinology (S.S.), National Institute of Arthritis, Metabolism and Digestive Diseases, National Institutes of Health, Bethesda, Maryland 20205. Received September 23, 1980. low dielectric macromolecular interior and van der Waals' interactions introduced as a consequence of the hydrophobic effect are the most important factors contributing to the observed negative values of AHo and ASo and hence to the stability of protein association complexes. The X-ray crystallographic structures of these complexes are consonant with this analysis. The tendency for protein association reactions to become entropy dominated and/or entropy-enthalpy assisted at low temperatures and enthalpy dominated at high temperatures (a consequence of the typically negative values of AC,\") arises from the diminution of the hydrophobic effect with increasing temperature which is a general property of the solvent, water. with small molecular substrates has become available. Concomitantly, X-ray crystallography has provided a detailed picture of some of these associations, and this has stimulated a number of theoretical studies (Levitt & Warshel, 1975; Gelin & Karplus, 1975; Chothia & Janin, 1975), based upon energetic considerations, to account for these structures. The This article not subject to U S . Copyright. Published 1981 by the American Chemical Society T H E R M O D Y N A M I C S O F P R O T E I N A S S O C I A T I O N V O L . 2 0 , N O . 1 1 , 1 9 8 1 3097 Table I: Thermodynamics of Protein Association' association process A G \" ~ AiY A s o , A c p o (kcal mol-') (kcal mol-l) (cal K-I mol-') (cal K-I mol-I) refb trypsin (bovine) + inhibitor (soybean) -14.6 8.6 78 -440 c, d deoxyhemoglobin S gelation -3.4 2.0 18 -200 e, f lysozyme self-association (indefinite) -3.9 -6 .4 -8.3 g glucagon trimerization -12.1 -3 1 -64 -430 h, i hemoglobin t haptoglobin -11.5 -3 3 -7 3 -940 i a-chymotrypsin dimerization -7.1 -35 -9 5 k, I S-peptide + S-protein (ribonuclease) -13 -40 -90 -1100 m, n All thermodynamic parameters expressed per mole of complex formed except the indefinite association cases of hemoglobin S and lysozyme for which the mole refers to the monomeric protein reacted. Unitary entropy and free energy are given for processes of defined stoichiometry. Standard states are hypothetical 1 M protein, pH at which the reaction was measured. All pHs were close to 7 except for trypsin, pH 5, haptoglobin, pH 5.5, and glucagon, pH 10.5. All data for 25 \"C except glucagon, T = 30 \"C. ence is to calorimetric work and the second is to X-ray crystallographic structure determination. al. (1974). e Rosset al. (1977). Wishner e t al. (1975). g Banerjee et al. (1975). Johnson et al. (1979). * Sasaki et al. (1975). For each entry, the first referSweet et Baugh & Trowbridge (1972). Lavialle et al. (1974). Shiao & Sturtevant (1969). lVandlen &Tulinsky (1973). Hearn et al. (1971). Wyckoff e t al. (1970). methodology and problems involved in such calculations have been critically reviewed by NBmethy & Scheraga (1977). In this paper we review the thermodynamics of protein association processes for the examples best characterized in terms of their chemistry and structure. From this survey we find that the thermodynamic parameters AGO, Ai?, AS\", and ACpo are predominantly of negative sign. This result poses severe difficulties for interpretations of protein association based upon the entropically driven hydrophobic effect. The aim of this paper is to attempt to account for the signs and magnitudes of these thermodynamic parameters for protein association reactions in terms of known molecular forces and the thermochemistry of small molecule interactions. read more read less
4,576 Citations
open accessOpen access Journal Article DOI: 10.1021/BI00483A001
Dominant forces in protein folding
Ken A. Dill1
07 Aug 1990 - Biochemistry

Abstract:

T e purpose of this review is to assess the nature and magnitudes of the dominant forces in protein folding. Since proteins are only marginally stable at room temperature,’ no type of molecular interaction is unimportant, and even small interactions can contribute significantly (positively or negatively) to stability (Alber, ... T e purpose of this review is to assess the nature and magnitudes of the dominant forces in protein folding. Since proteins are only marginally stable at room temperature,’ no type of molecular interaction is unimportant, and even small interactions can contribute significantly (positively or negatively) to stability (Alber, 1989a,b; Matthews, 1987a,b). However, the present review aims to identify only the largest forces that lead to the structural features of globular proteins: their extraordinary compactness, their core of nonpolar residues, and their considerable amounts of internal architecture. This review explores contributions to the free energy of folding arising from electrostatics (classical charge repulsions and ion pairing), hydrogen-bonding and van der Waals interactions, intrinsic propensities, and hydrophobic interactions. An earlier review by Kauzmann (1959) introduced the importance of hydrophobic interactions. His insights were particularly remarkable considering that he did not have the benefit of known protein structures, model studies, high-resolution calorimetry, mutational methods, or force-field or statistical mechanical results. The present review aims to provide a reassessment of the factors important for folding in light of current knowledge. Also considered here are the opposing forces, conformational entropy and electrostatics. The process of protein folding has been known for about 60 years. In 1902, Emil Fischer and Franz Hofmeister independently concluded that proteins were chains of covalently linked amino acids (Haschemeyer & Haschemeyer, 1973) but deeper understanding of protein structure and conformational change was hindered because of the difficulty in finding conditions for solubilization. Chick and Martin (191 1) were the first to discover the process of denaturation and to distinguish it from the process of aggregation. By 1925, the denaturation process was considered to be either hydrolysis of the peptide bond (Wu & Wu, 1925; Anson & Mirsky, 1925) or dehydration of the protein (Robertson, 1918). The view that protein denaturation was an unfolding process was read more read less

Topics:

Protein folding (59%)59% related to the paper, Lattice protein (56%)56% related to the paper, Globular protein (55%)55% related to the paper, Protein structure (55%)55% related to the paper, Hydrophobic collapse (52%)52% related to the paper
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3,570 Citations
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Biochemistry format uses ACS Custom Citation (achemso) citation style.

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Frequently asked questions

1. Can I write Biochemistry in LaTeX?

Absolutely not! Our tool has been designed to help you focus on writing. You can write your entire paper as per the Biochemistry guidelines and auto format it.

2. Do you follow the Biochemistry guidelines?

Yes, the template is compliant with the Biochemistry 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 Biochemistry?

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 Biochemistry citation style.

4. Can I use the Biochemistry templates for free?

Sign up for our free trial, and you'll be able to use all our features for seven days. You'll see how helpful they are and how inexpensive they are compared to other options, Especially for Biochemistry.

5. Can I use a manuscript in Biochemistry that I have written in MS Word?

Yes. You can choose the right template, copy-paste the contents from the word document, and click on auto-format. Once you're done, you'll have a publish-ready paper Biochemistry that you can download at the end.

6. How long does it usually take you to format my papers in Biochemistry?

It only takes a matter of seconds to edit your manuscript. Besides that, our intuitive editor saves you from writing and formatting it in Biochemistry.

7. Where can I find the template for the Biochemistry?

It is possible to find the Word template for any journal on Google. However, why use a template when you can write your entire manuscript on SciSpace , auto format it as per Biochemistry's guidelines and download the same in Word, PDF and LaTeX formats? Give us a try!.

8. Can I reformat my paper to fit the Biochemistry's guidelines?

Of course! You can do this using our intuitive editor. It's very easy. If you need help, our support team is always ready to assist you.

9. Biochemistry an online tool or is there a desktop version?

SciSpace's Biochemistry is currently available as an online tool. We're developing a desktop version, too. You can request (or upvote) any features that you think would be helpful for you and other researchers in the "feature request" section of your account once you've signed up with us.

10. I cannot find my template in your gallery. Can you create it for me like Biochemistry?

Sure. You can request any template and we'll have it setup within a few days. You can find the request box in Journal Gallery on the right side bar under the heading, "Couldn't find the format you were looking for like Biochemistry?”

11. What is the output that I would get after using Biochemistry?

After writing your paper autoformatting in Biochemistry, you can download it in multiple formats, viz., PDF, Docx, and LaTeX.

12. Is Biochemistry's impact factor high enough that I should try publishing my article there?

To be honest, the answer is no. The impact factor is one of the many elements that determine the quality of a journal. Few of these factors include review board, rejection rates, frequency of inclusion in indexes, and Eigenfactor. You need to assess all these factors before you make your final call.

13. What is Sherpa RoMEO Archiving Policy for Biochemistry?

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 Biochemistry. 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 Biochemistry?

The 5 most common citation types in order of usage for Biochemistry are:.

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

15. How do I submit my article to the Biochemistry?

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16. Can I download Biochemistry 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 Biochemistry Endnote style according to Elsevier guidelines.

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