@article{SchnabelSchnabelBerndt1971,
  author    = {Schnabel, Eugen and Schnabel, Henning and Berndt, Heinz},
  title     = {Zur selektiven acidolytischen Abspaltbarkeit der tert.-Butyloxycarbonyl-Gruppe},
  series = {Justus Liebigs Annalen der Chemie},
  volume    = {749},
  journal   = {Justus Liebigs Annalen der Chemie},
  number    = {1},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1099-0690},
  doi       = {10.1002/jlac.19717490111},
  pages     = {90 -- 108},
  year      = {1971},
  abstract  = {Die tert.-Butyloxycarbonyl-Gruppe (Boc) l{\"a}ßt sich mittels reiner Trifluoressigs{\"a}ure nicht selektiv neben dem Benzyloxycarbonyl-Rest (Z) abspalten. Das gelingt auch nicht mit L{\"o}sungen von Trifluoressigs{\"a}ure bzw. Chlorwasserstoff in organischen L{\"o}sungsmitteln. Kern-substituierte Z-Gruppen wie Z(pCl), Z(mCl) oder Z(pNO₂) sind zwar stabiler, werden aber von den obengenannten Reagenzien ebenfalls angegriffen bzw. sind nicht mehr acidolytisch abspaltbar. - Mit 70proz. w{\"a}ßriger Trifluoressigs{\"a}ure gelingt die Abspaltung von Boc neben Z dagegen fast selektiv; dabei werden aber Benzylester, besonders Glutamins{\"a}ure-γ-benzylester, teilweise hydrolysiert, w{\"a}hrend Methyl- sowie {\"A}thylester nahezu best{\"a}ndig sind. Die Brauchbarkeit des Abspaltungsverfahrens wird anhand der schrittweise durchgef{\"u}hrten Synthese zweier Heptapeptid-Derivate gezeigt. - {\"A}hnlich spezifisch gelingt die Abspaltung von Boc mit Bortrifluorid-{\"a}therat in Eisessig; Benzylester sind gegen{\"u}ber diesem Reagenz stabiler als gegen w{\"a}ßrige Trifluoressigs{\"a}ure. Das Bortrifluorid-Verfahren eignet sich besonders f{\"u}r die Abspaltung von Boc-Gruppen neben s{\"a}urelabilen Thiol-Schutzgruppen (Tetrahydropyranyl- bzw. Trityl-Rest) sowie neben dem Cyclocystinyl-Rest. Die Leistungsf{\"a}higkeit der Methode wird durch die Synthese zweier Peptid-Derivate mit S-Trityl-Schutzgruppen belegt. Als Nebenreaktion ist die Acetylierung von aliphatischen Hydroxylgruppen m{\"o}glich. Sie l{\"a}ßt sich vermeiden, wenn man die Spaltung in anderen L{\"o}sungsmitteln durchf{\"u}hrt. Die als Modellverbindungen f{\"u}r Stabilit{\"a}tsuntersuchungen verwendeten Nε-acylierten Lysin-Derivate werden mit dem Aminos{\"a}ureanalysator quantitativ neben Lysin bestimmt.},
  language  = {de}
}
@article{NokiharaBerndt1978,
  author    = {Nokihara, Kiyoshi and Berndt, Heinz},
  title     = {Synthesis of hapten-polypeptide conjugates as antigen models for the N-terminal region of the α-2-chain of rabbit skin collagen},
  series = {Journal of the Royal Society of Chemistry: Perkin Transactions 1},
  volume    = {1978},
  journal   = {Journal of the Royal Society of Chemistry: Perkin Transactions 1},
  number    = {3},
  publisher = {Royal Society of Chemistry},
  address   = {Cambridge},
  issn      = {1364-5463},
  doi       = {10.1039/P19780000260},
  pages     = {260 -- 263},
  year      = {1978},
  abstract  = {Synthesis of derivatives of the peptide sequence L-pyroglutamyl-L-phenylalanyl-L-aspartyl-glycyl-L-lysyl-glycyl-glycyl-glycine as the antigenic determinant representing the N-terminal non-helical region of the α-2-chain of rabbit skin collagen, and conjugation to two different polypeptide carriers, are described.},
  language  = {en}
}
@article{NokiharaBerndt1979,
  author    = {Nokihara, Kiyoshi and Berndt, Heinz},
  title     = {Darstellung von Bis(S-methoxycarbonylthio)-B-Kette des Rinderinsulins},
  series = {Hoppe-Seyler's Zeitschrift f{\"u}r physiologische Chemie},
  volume    = {360},
  journal   = {Hoppe-Seyler's Zeitschrift f{\"u}r physiologische Chemie},
  number    = {1},
  issn      = {1437-4315},
  doi       = {10.1515/bchm2.1979.360.1.773},
  pages     = {773 -- 776},
  year      = {1979},
  language  = {de}
}
@article{Berndt1979,
  author    = {Berndt, Heinz},
  title     = {Synthese der Sequenz 71—86 des Humanproinsulins, III : Synthese {\"u}ber die Fragmente 71—78 und 79—86},
  series = {Hoppe-Seyler's Zeitschrift f{\"u}r physiologische Chemie},
  volume    = {360},
  journal   = {Hoppe-Seyler's Zeitschrift f{\"u}r physiologische Chemie},
  number    = {1},
  issn      = {1437-4315},
  doi       = {10.1515/bchm2.1979.360.1.765},
  pages     = {765 -- 772},
  year      = {1979},
  language  = {de}
}
@article{Berndt1979,
  author    = {Berndt, Heinz},
  title     = {Synthese der Sequenz 71—86 des Humanproinsulins, I : Synthese der Sequenz 71—86 als monomeres cyclisches Biscystinpeptidderivat und als Tetra-S-tritylderivat},
  series = {Hoppe-Seyler's Zeitschrift f{\"u}r physiologische Chemie},
  volume    = {360},
  journal   = {Hoppe-Seyler's Zeitschrift f{\"u}r physiologische Chemie},
  number    = {1},
  issn      = {1437-4315},
  doi       = {10.1515/bchm2.1979.360.1.747},
  pages     = {747 -- 760},
  year      = {1979},
  language  = {de}
}
@article{NaithaniKlostermeyerLangeetal.1971,
  author    = {Naithani, V. K and Klostermeyer, Henning and Lange, H. R. and [u.a.], and Berndt, Heinz and [u.a.],},
  title     = {Preparation of peptide derivatives for porcine proinsulin-synthesis},
  series = {Biological Chemistry},
  volume    = {352},
  journal   = {Biological Chemistry},
  number    = {1},
  publisher = {De Gruyter},
  issn      = {1437-4315},
  doi       = {10.1515/bchm2.1971.352.1.1},
  pages     = {2 -- 3},
  year      = {1971},
  language  = {en}
}
@article{MatoniBerndt1980,
  author    = {Matoni, Georg and Berndt, Heinz},
  title     = {Thermal synthesis of the optical pure pentapeptide derivative Z-(L)-Ala-(L)-Phe-Gly-(L)-Phe-Gly-OMe},
  series = {Tetrahedron letters},
  volume    = {21},
  journal   = {Tetrahedron letters},
  number    = {1},
  issn      = {0040-4039},
  doi       = {10.1016/S0040-4039(00)93618-9},
  pages     = {37 -- 40},
  year      = {1980},
  language  = {en}
}
@article{NokiharaBerndt1978,
  author    = {Nokihara, Kiyoshi and Berndt, Heinz},
  title     = {Studies on sulfur-containing peptides : tert-butyloxycarbonylsulfenyl and benzyloxycarbonylsulfenyl derivatives as protecting groups for cysteine},
  series = {The journal of organic chemistry},
  volume    = {43},
  journal   = {The journal of organic chemistry},
  number    = {25},
  publisher = {American Chemical Society},
  address   = {Washington},
  issn      = {0022-3263},
  doi       = {10.1021/jo00419a046},
  pages     = {4893 -- 4895},
  year      = {1978},
  language  = {en}
}
@article{BerndtGattnerZahn1975,
  author    = {Berndt, Heinz and Gattner, Hans-Gregor and Zahn, Helmut},
  title     = {Semisynthetisches Des-A1-glycin-Schafinsulin},
  series = {Biological Chemistry},
  volume    = {356},
  journal   = {Biological Chemistry},
  number    = {2},
  publisher = {De Gruyter},
  address   = {Berlin},
  issn      = {1437-4315},
  doi       = {10.1515/bchm2.1975.356.2.1455},
  pages     = {1469 -- 1472},
  year      = {1975},
  language  = {de}
}
@article{BerndtZahn1975,
  author    = {Berndt, Heinz and Zahn, Helmut},
  title     = {Peptide, 99 : Monomere cyclische Cystinpeptidderivate, III ; Synthese der Schafinsulin-A-Kettensequenzen A2-21 und A1-21 als monomere cyclische Dicystinpeptidderivate},
  series = {Justus Liebigs Annalen der Chemie},
  volume    = {1975},
  journal   = {Justus Liebigs Annalen der Chemie},
  number    = {9},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1099-0690},
  doi       = {10.1002/jlac.197519750908},
  pages     = {1601 -- 1612},
  year      = {1975},
  abstract  = {Die Synthese der Sequenzen A2—21 (13) und A1—21 (15) der Schafinsulin-A-Kette als monomere cyclische Dicystinpeptidderivate wird beschrieben. Die intrachenaren Cystinbr{\"u}cken A6—7 und A 11 —20 vermitteln die L{\"o}slichkeit dieser Derivate in Dimethylformamid und erm{\"o}glichen erstmalig die Reindarstellung vollgesch{\"u}tzter Insulin-A-Kettenderivate. Die w{\"a}hrend der Synthese eingesetzten Schutzgruppen lassen sich mittels Trifluoressigs{\"a}ure und 2-Mercapto{\"a}thanol quantitativ entfernen.},
  language  = {de}
}
@article{SchwertnerBerndtGielenetal.1975,
  author    = {Schwertner, Eberhard and Berndt, Heinz and Gielen, Hans-G{\"u}nter and Zahn, Helmut},
  title     = {Peptide 96 : Synthese einiger [2-(p-Biphenylyl)isopropyloxycarbonyl]-Aminos{\"a}urederivate},
  series = {Justus Liebigs Annalen der Chemie},
  volume    = {75},
  journal   = {Justus Liebigs Annalen der Chemie},
  number    = {3},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1099-0690},
  doi       = {10.1002/jlac.197519750318},
  pages     = {581 -- 585},
  year      = {1975},
  abstract  = {Die Darstellung der N-[2-(p-Biphenylyl)isopropyloxycarbonyl]-Derivate (Bpoc-Derivate) des Cysteins unter Verwendung der Thiolschutzgruppen Tetrahydropyranyl (Thp) f{\"u}r 1, Diphenylmethyl (Dpm) f{\"u}r 2, Trityl (Trt) f{\"u}r 3 und S-tert.-Butyl (SBut) f{\"u}r 4 sowie die Synthese von aktivierten Estern der Bpoc-Derivate des Glycins (5), Isoleucins (6) und Prolins (7) werden beschrieben. An einem Beispiel wird die M{\"o}glichkeit aufgezeigt, die Bpoc-Gruppe {\"u}ber das Bpoc-Azid nachtr{\"a}glich in den Peptidverband einzuf{\"u}hren.},
  language  = {de}
}
@article{TurckBerndt1981,
  author    = {Turck, Christoph W. and Berndt, Heinz},
  title     = {Synthese definierter Peptid-Derivate durch Aminolyse von 3-(Nα-Acyl-peptidyloxy)-2-hydroxy-N-alkylbenzamiden bei erh{\"o}hten Temperaturen, I : Synthese des Modellpeptid-Derivates Z-Ala-Phe-Gly-N(Et)2},
  series = {Hoppe-Seyler´s Zeitschrift f{\"u}r physiologische Chemie},
  volume    = {362},
  journal   = {Hoppe-Seyler´s Zeitschrift f{\"u}r physiologische Chemie},
  number    = {1},
  issn      = {1437-4315},
  doi       = {10.1515/bchm2.1981.362.1.821},
  pages     = {821 -- 828},
  year      = {1981},
  language  = {de}
}
@article{DanhoNaithaniSasakietal.1980,
  author    = {Danho, Waleed and Naithani, Vinod K. and Sasaki, Andr{\´e} N. and F{\"o}hles, Joseph and Berndt, Heinz and [u.a.],},
  title     = {Human proinsulin, VII : synthesis of two protected peptides corresponding to the sequences 1—45 and 46—86 of the prohormone},
  series = {Hoppe-Seyler's Zeitschrift f{\"u}r physiologische Chemie},
  volume    = {361},
  journal   = {Hoppe-Seyler's Zeitschrift f{\"u}r physiologische Chemie},
  number    = {1},
  issn      = {1437-4315},
  doi       = {10.1515/bchm2.1980.361.1.857},
  pages     = {857 -- 863},
  year      = {1980},
  language  = {en}
}
@article{WolfBerndtBrandenburg1979,
  author    = {Wolf, G{\"u}nter and Berndt, Heinz and Brandenburg, Dietrich},
  title     = {Synthese der [LysA13] Rinderinsulin-A-Kette in der Form [Lys(Tfa)A13]A(SO3H)4 und NαA1-Msc-[LysA13]A(SO3H)4 unter Verwendung des S-tert-Butylmercapto-Restes als Thiolschutzgruppe},
  series = {Hoppe-Seyler's Zeitschrift f{\"u}r physiologische Chemie},
  volume    = {360},
  journal   = {Hoppe-Seyler's Zeitschrift f{\"u}r physiologische Chemie},
  number    = {2},
  issn      = {1437-4315},
  doi       = {10.1515/bchm2.1979.360.2.1569},
  pages     = {1569 -- 1578},
  year      = {1979},
  language  = {de}
}
@article{WilhelmBerndtBrandenburg1979,
  author    = {Wilhelm, Wolff and Berndt, Heinz and Brandenburg, Dietrich},
  title     = {Zur Synthese der H{\"u}hnerinsulin-A-Kette, I : Darstellung der Fragmente A1-8, A9-15, A1-7 und A8-15},
  series = {Hoppe-Seyler's Zeitschrift f{\"u}r physiologische Chemie},
  volume    = {360},
  journal   = {Hoppe-Seyler's Zeitschrift f{\"u}r physiologische Chemie},
  number    = {2},
  issn      = {1437-4315},
  doi       = {10.1515/bchm2.1979.360.2.1559},
  pages     = {1559 -- 1568},
  year      = {1979},
  language  = {de}
}
@article{WolfBerndtBrandenburg1979,
  author    = {Wolf, Wilhelm and Berndt, Heinz and Brandenburg, Dietrich},
  title     = {Synthese von Fragmenten einer [LysA13] Rinder-Insulin-A-Kette unter Verwendung des S-tert-Butylmercaptorestes als Thiolschutz},
  series = {Hoppe-Seyler's Zeitschrift f{\"u}r physiologische Chemie},
  volume    = {360},
  journal   = {Hoppe-Seyler's Zeitschrift f{\"u}r physiologische Chemie},
  number    = {2},
  issn      = {1437-4315},
  doi       = {10.1515/bchm2.1979.360.2.1549},
  pages     = {1549 -- 1558},
  year      = {1979},
  language  = {de}
}
@article{GielenWolfBerndtetal.1979,
  author    = {Gielen, Hans-G{\"u}nther and Wolf, G{\"u}nter and Berndt, Heinz and Zahn, Helmut},
  title     = {Synthese der Fragmente A1-8, A9-15 und A16-21 der Schafinsulin-A-Kette unter Verwendung des S-tert-Butylmercaptorestes als Thiolschutzgruppe},
  series = {Hoppe-Seyler's Zeitschrift f{\"u}r physiologische Chemie},
  volume    = {360},
  journal   = {Hoppe-Seyler's Zeitschrift f{\"u}r physiologische Chemie},
  number    = {2},
  issn      = {1437-4315},
  doi       = {10.1515/bchm2.1979.360.2.1535},
  pages     = {1535 -- 1548},
  year      = {1979},
  language  = {de}
}
@article{BerndtKrueger1985,
  author    = {Berndt, Heinz and Kr{\"u}ger, G{\"o}tz},
  title     = {Resolution of enantiomeric amino acid derivatives by high-performance liquid chromatography on chiral stationary phases},
  series = {Journal of chromatography A},
  volume    = {1985},
  journal   = {Journal of chromatography A},
  number    = {348},
  issn      = {0021-9673},
  doi       = {10.1016/S0021-9673(01)92461-6},
  pages     = {275 -- 279},
  year      = {1985},
  language  = {en}
}
@article{WangDruckenmuellerElbersetal.2014,
  author    = {Wang, Ren-Qi and Druckenm{\"u}ller, Katharina and Elbers, Gereon and Guenther, Klaus and Crou{\´e}, Jean-Philippe},
  title     = {Analysis of aquatic-phase natural organic matter by optimized LDI-MS method},
  series = {Journal of mass spectrometry},
  volume    = {49},
  journal   = {Journal of mass spectrometry},
  number    = {2},
  publisher = {Wiley},
  address   = {Bognor Regis},
  issn      = {1096-9888},
  doi       = {10.1002/jms.3321},
  pages     = {154 -- 160},
  year      = {2014},
  abstract  = {The composition and physiochemical properties of aquatic-phase natural organic matter (NOM) are most important problems for both environmental studies and water industry. Laser desorption/ionization (LDI) mass spectrometry facilitated successful examinations of NOM, as humic and fulvic acids in NOM are readily ionized by the nitrogen laser. In this study, hydrophobic NOMs (HPO NOMs) from river, reservoir and waste water were characterized by this technique. The effect of analytical variables like concentration, solvent composition and laser energy was investigated. The exact masses of small molecular NOM moieties in the range of 200-1200 m/z were determined in reflectron mode. In addition, spectra of post-source-decay experiments in this range showed that some compounds from different natural NOMs had the same fragmental ions. In the large mass range of 1200-15 000 Da, macromolecules and their aggregates were found in HPO NOMs from natural waters. Highly humic HPO exhibited mass peaks larger than 8000 Da. On the other hand, the waste water and reservoir water mainly had relatively smaller molecules of about 2000 Da. The LDI-MS measurements indicated that highly humic river waters were able to form large aggregates and membrane foulants, while the HPO NOMs from waste water and reservoir water were unlikely to form large aggregates. Copyright © 2014 John Wiley \& Sons, Ltd.},
  language  = {en}
}
@article{HeineHerrmannSelmeretal.2014,
  author    = {Heine, A. and Herrmann, G. and Selmer, Thorsten and Terwesten, F. and Buckel, W. and Reuter, K.},
  title     = {High resolution crystal structure of clostridium propionicum β-Alanyl-CoA:Ammonia Lyase, a new member of the "Hot Dog Fold" protein superfamily},
  series = {Proteins},
  volume    = {82},
  journal   = {Proteins},
  number    = {9},
  publisher = {Wiley-Liss},
  address   = {New York},
  issn      = {1097-0134 (E-Journal); 0887-3585 (Print)},
  doi       = {10.1002/prot.24557},
  pages     = {2041 -- 2053},
  year      = {2014},
  abstract  = {Clostridium propionicum is the only organism known to ferment β-alanine, a constituent of coenzyme A (CoA) and the phosphopantetheinyl prosthetic group of holo-acyl carrier protein. The first step in the fermentation is a CoA-transfer to β-alanine. Subsequently, the resulting β-alanyl-CoA is deaminated by the enzyme β-alanyl-CoA:ammonia lyase (Acl) to reversibly form ammonia and acrylyl-CoA. We have determined the crystal structure of Acl in its apo-form at a resolution of 0.97 {\AA} as well as in complex with CoA at a resolution of 1.59 {\AA}. The structures reveal that the enyzme belongs to a superfamily of proteins exhibiting a so called "hot dog fold" which is characterized by a five-stranded antiparallel β-sheet with a long α-helix packed against it. The functional unit of all "hot dog fold" proteins is a homodimer containing two equivalent substrate binding sites which are established by the dimer interface. In the case of Acl, three functional dimers combine to a homohexamer strongly resembling the homohexamer formed by YciA-like acyl-CoA thioesterases. Here, we propose an enzymatic mechanism based on the crystal structure of the Acl·CoA complex and molecular docking. Proteins 2014; 82:2041-2053. © 2014 Wiley Periodicals, Inc.},
  language  = {en}
}