kokomiko
14-10-2013, 14:18
Hallo,
ich schlage mich schon seit einiger Zeit mit dem Stil von meinem Literaturverzeichnis rum, hab auch schon ein paar Antworten durch googeln gefunden, aber mir fehlen noch ein paar Kleinigkeiten.
Ich verwalte meine Referenzen mit JabRef.
\documentclass[a4paper, 11pt] {scrartcl}
%Bibliothek
\usepackage[backend=biber, style=authoryear, bibstyle=authoryear,
mergedate=false, dashed=false, natbib=true, url=false,
doi=false, eprint=false]{biblatex}
\begin{filecontents}{\jobname.bib}
@ARTICLE{Hunsicker-Wang2003,
author = {Hunsicker-Wang, Laura M. and Heine, Andreas and Chen, Ying and Luna,
Eugene P. and Todaro, Thomas and Zhang, Yan Ming and Williams, Pamela
A. and McRee, Duncan E. and Hirst, Judy and Stout, C David and Fee,
James A.},
title = {High-resolution structure of the soluble, respiratory-type Rieske
protein from Thermus thermophilus: analysis and comparison.},
journal = {Biochemistry},
year = {2003},
volume = {42},
pages = {7303--7317},
number = {24},
month = {Jun},
abstract = {The structure of the soluble Rieske protein from Thermus thermophilus
has been determined at a resolution of 1.3 A at pH 8.5 using multiwavelength
anomalous dispersion (MAD) techniques. This is the first report of
a Rieske protein from a menaquinone-utilizing organism. The structure
shows an overall fold similar to previously reported Rieske proteins.
A novel feature of this crystal form appears to be a shared hydrogen
between the His-134 imidazole ring ligated to Fe2 of the [2Fe-2S]
cluster and its symmetry partner, His-134', one being formally an
imidazolate anion, Fe2-(His-134)N(epsilon)(-)...H-N(epsilon')(His-134')-Fe2',
in which crystallographic C(2) axes pass equidistant between N(epsilon)...N(epsilon')
and normal to the line defined by N(epsilon)...N(epsilon'). This
provides evidence for a stable, oxidized cluster with a His(-) ligand
and lends support to a previously proposed mechanism of coupled proton
and electron transfer. A detailed comparison of the Thermus Rieske
protein with six other Rieske and Rieske-type proteins indicates:
(a) The cluster binding domain is tightly conserved. (b) The 3-D
structure of the 10 beta-strand fold is conserved, even among the
most divergent proteins. (c) There is an approximately linear relation
between acid-pH redox potential and number of H-bonds to the cluster.
(d) These proteins have two faces, one points into the larger complex
(bc(1), b(6)f, or other), is involved in the proton coupled electron
transfer function, and is highly conserved. The second is oriented
toward the solvent and shows wide variation in charge, sequence,
length, hydrophobicity, and secondary elements in the loops that
connect the beta-sheets.},
doi = {10.1021/bi0342719},
institution = {Division of Biology, the University of California at San Diego, 9500
Gilman Drive, La Jolla, California 92093, USA.},
keywords = {Amino Acid Sequence; Crystallography, X-Ray, methods; Electron Transport
Complex III; Hydrogen Bonding; Iron-Sulfur Proteins, analysis/chemistry/genetics/metabolism;
Models, Molecular; Molecular Sequence Data; Probability; Protein
Binding; Protein Structure, Secondary; Protein Structure, Tertiary;
Sequence Homology, Amino Acid; Solubility; Static Electricity; Thermus
thermophilus, chemistry},
language = {eng},
medline-pst = {ppublish},
owner = {},
pmid = {12809486},
timestamp = {2013.10.09},
url = {http://dx.doi.org/10.1021/bi0342719}
@ARTICLE{Neuberg1913,
author = {Neuberg, C and Kerb, J.},
title = {Zur Frage der Aldehydbildung bei der Gärung von Hexosen sowie bei
der sog. Selbstgärung.},
journal = {Biochem Zeitschr},
year = {1913},
volume = {58},
pages = {158-170},
owner = {},
timestamp = {2013.10.07}
}
}
\end{filecontents}
% Bibliografie laden
\addbibresource{\jobname.bib}
\DefineBibliographyStrings{english}{andothers={et\ addabbrvspace al\adddot}}
\begin{document}
BLABLABLA \textcite{Hunsicker-Wang2003}.
\printbibliography
\end{document}
Ausgabe
BLABLABLA Hunsicker-Wang et al. (2003).
References
Hunsicker-Wang, Laura M. et al. (2003). "High-resolution structure of the soluble, respiratory-type Rieske protein from Thermus thermophilus: analysis and comparison." eng. In:
Biochemistry 42.24 (June 2003), pp. 7303-7317.
Neuberg, C and J. Kerb (1913). ‘Zur Frage der Aldehydbildung bei der Gärung von Hexosen
sowie bei der sog. Selbstgärung.’ In: Biochem Zeitschr 58 (1913), pp. 158–170.
Die Zitierung im Text ist soweit ok. Was ich ändern möchte ist
anstatt et al. sollen im Literaturverzeichen alle Namen der Autoren aufgelistet werden
Der Vorname soll auf einen einzelnen Buchstaben und Punkt abgekürzt werden
number (im Beispiel "24") soll in Klammern
es soll lediglich am Anfang hinter die Autorennamen das Jahr und eventuell 2003b (wenn es zweimal dieselben Autoren im selben Jahr sind) und das zweiten (June 2003) weg
die Angabe der Sprache soll weg (im ersten Beispiel: "eng." -->language=false hat nicht funktioniert :confused:)
das "In:" weg
Alle Namen sollen immer in Nachname, V. aufgeführt werden (Momentan ist der erste richtig, der zweite falsch (Beispiel Neuberg+Kerb))
Kann mir jemand helfen?
ich schlage mich schon seit einiger Zeit mit dem Stil von meinem Literaturverzeichnis rum, hab auch schon ein paar Antworten durch googeln gefunden, aber mir fehlen noch ein paar Kleinigkeiten.
Ich verwalte meine Referenzen mit JabRef.
\documentclass[a4paper, 11pt] {scrartcl}
%Bibliothek
\usepackage[backend=biber, style=authoryear, bibstyle=authoryear,
mergedate=false, dashed=false, natbib=true, url=false,
doi=false, eprint=false]{biblatex}
\begin{filecontents}{\jobname.bib}
@ARTICLE{Hunsicker-Wang2003,
author = {Hunsicker-Wang, Laura M. and Heine, Andreas and Chen, Ying and Luna,
Eugene P. and Todaro, Thomas and Zhang, Yan Ming and Williams, Pamela
A. and McRee, Duncan E. and Hirst, Judy and Stout, C David and Fee,
James A.},
title = {High-resolution structure of the soluble, respiratory-type Rieske
protein from Thermus thermophilus: analysis and comparison.},
journal = {Biochemistry},
year = {2003},
volume = {42},
pages = {7303--7317},
number = {24},
month = {Jun},
abstract = {The structure of the soluble Rieske protein from Thermus thermophilus
has been determined at a resolution of 1.3 A at pH 8.5 using multiwavelength
anomalous dispersion (MAD) techniques. This is the first report of
a Rieske protein from a menaquinone-utilizing organism. The structure
shows an overall fold similar to previously reported Rieske proteins.
A novel feature of this crystal form appears to be a shared hydrogen
between the His-134 imidazole ring ligated to Fe2 of the [2Fe-2S]
cluster and its symmetry partner, His-134', one being formally an
imidazolate anion, Fe2-(His-134)N(epsilon)(-)...H-N(epsilon')(His-134')-Fe2',
in which crystallographic C(2) axes pass equidistant between N(epsilon)...N(epsilon')
and normal to the line defined by N(epsilon)...N(epsilon'). This
provides evidence for a stable, oxidized cluster with a His(-) ligand
and lends support to a previously proposed mechanism of coupled proton
and electron transfer. A detailed comparison of the Thermus Rieske
protein with six other Rieske and Rieske-type proteins indicates:
(a) The cluster binding domain is tightly conserved. (b) The 3-D
structure of the 10 beta-strand fold is conserved, even among the
most divergent proteins. (c) There is an approximately linear relation
between acid-pH redox potential and number of H-bonds to the cluster.
(d) These proteins have two faces, one points into the larger complex
(bc(1), b(6)f, or other), is involved in the proton coupled electron
transfer function, and is highly conserved. The second is oriented
toward the solvent and shows wide variation in charge, sequence,
length, hydrophobicity, and secondary elements in the loops that
connect the beta-sheets.},
doi = {10.1021/bi0342719},
institution = {Division of Biology, the University of California at San Diego, 9500
Gilman Drive, La Jolla, California 92093, USA.},
keywords = {Amino Acid Sequence; Crystallography, X-Ray, methods; Electron Transport
Complex III; Hydrogen Bonding; Iron-Sulfur Proteins, analysis/chemistry/genetics/metabolism;
Models, Molecular; Molecular Sequence Data; Probability; Protein
Binding; Protein Structure, Secondary; Protein Structure, Tertiary;
Sequence Homology, Amino Acid; Solubility; Static Electricity; Thermus
thermophilus, chemistry},
language = {eng},
medline-pst = {ppublish},
owner = {},
pmid = {12809486},
timestamp = {2013.10.09},
url = {http://dx.doi.org/10.1021/bi0342719}
@ARTICLE{Neuberg1913,
author = {Neuberg, C and Kerb, J.},
title = {Zur Frage der Aldehydbildung bei der Gärung von Hexosen sowie bei
der sog. Selbstgärung.},
journal = {Biochem Zeitschr},
year = {1913},
volume = {58},
pages = {158-170},
owner = {},
timestamp = {2013.10.07}
}
}
\end{filecontents}
% Bibliografie laden
\addbibresource{\jobname.bib}
\DefineBibliographyStrings{english}{andothers={et\ addabbrvspace al\adddot}}
\begin{document}
BLABLABLA \textcite{Hunsicker-Wang2003}.
\printbibliography
\end{document}
Ausgabe
BLABLABLA Hunsicker-Wang et al. (2003).
References
Hunsicker-Wang, Laura M. et al. (2003). "High-resolution structure of the soluble, respiratory-type Rieske protein from Thermus thermophilus: analysis and comparison." eng. In:
Biochemistry 42.24 (June 2003), pp. 7303-7317.
Neuberg, C and J. Kerb (1913). ‘Zur Frage der Aldehydbildung bei der Gärung von Hexosen
sowie bei der sog. Selbstgärung.’ In: Biochem Zeitschr 58 (1913), pp. 158–170.
Die Zitierung im Text ist soweit ok. Was ich ändern möchte ist
anstatt et al. sollen im Literaturverzeichen alle Namen der Autoren aufgelistet werden
Der Vorname soll auf einen einzelnen Buchstaben und Punkt abgekürzt werden
number (im Beispiel "24") soll in Klammern
es soll lediglich am Anfang hinter die Autorennamen das Jahr und eventuell 2003b (wenn es zweimal dieselben Autoren im selben Jahr sind) und das zweiten (June 2003) weg
die Angabe der Sprache soll weg (im ersten Beispiel: "eng." -->language=false hat nicht funktioniert :confused:)
das "In:" weg
Alle Namen sollen immer in Nachname, V. aufgeführt werden (Momentan ist der erste richtig, der zweite falsch (Beispiel Neuberg+Kerb))
Kann mir jemand helfen?