Zobrazeno 1 - 10 of 567 pro vyhledávání: '"Luis Moroder"'
1
Chemical synthesis of per ‐selenocysteine human epidermal growth factor
Autor: Toshiki Takei, Hideaki Tanaka, Nobuaki Okumura, Toshifumi Takao, Luis Moroder, Hironobu Hojo
Publikováno v: Journal of Peptide Science. 29
Human seleno-epidermal growth factor (seleno-EGF), a 53-residue peptide where all six cysteine residues of the parent human EGF sequence were replaced by selenocysteines, was synthesized and the oxidative folding of a polypeptide containing three dis
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0f5bc07a16534bbaf5e603284dcbd0a1
https://doi.org/10.1002/psc.3464
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3
Review
Autor: Luis Moroder, Hans-Jürgen Musiol
Publikováno v: JOURNAL OF PEPTIDE SCIENCE
The chalcogen elements oxygen, sulfur, and selenium are essential constituents of side chain functions of natural amino acids. Conversely, no structural and biological function has been discovered so far for the heavier and more metallic tellurium el
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::44995dfd0268405426b4e614b4be271d
https://hdl.handle.net/21.11116/0000-0005-A122-E21.11116/0000-0005-A124-C
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4
Time-resolved infrared studies of the unfolding of a light triggered β-hairpin peptide
Autor: Wolfgang Zinth, Michael S. Rampp, Tom Podewin, Anja Hoffmann-Röder, Luis Moroder, Stefan M. Hofmann
Publikováno v: Chemical Physics. 512:116-121
The light triggered unfolding reaction of the azobenzene peptide AzoTrpZip2 is investigated from 1 ps to 100 µs. Absorption changes show that the unfolding is a multistep process with the initial breaking of the hydrogen bonds in the vicinity of the
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::354d3c88fc28f2b7a85ecc86852992c5
https://doi.org/10.1016/j.chemphys.2018.02.003
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5
Akademický článek
Synthetic biology of proteins: tuning GFPs folding and stability with fluoroproline.
Autor: Thomas Steiner, Petra Hess, Jae Hyun Bae, Birgit Wiltschi, Luis Moroder, Nediljko Budisa
Publikováno v: PLoS ONE, Vol 3, Iss 2, p e1680 (2008)
Proline residues affect protein folding and stability via cis/trans isomerization of peptide bonds and by the C(gamma)-exo or -endo puckering of their pyrrolidine rings. Peptide bond conformation as well as puckering propensity can be manipulated by
Externí odkaz: https://doaj.org/article/c7633bf2862148b0a07f7db4fdf3333b
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6
Insulin-From its Discovery to the Industrial Synthesis of Modern Insulin Analogues
Autor: Hans-Jürgen Musiol, Luis Moroder
Publikováno v: Angewandte Chemie International Edition. 56:10656-10669
After the discovery of insulin as a drug for diabetes, the pharmaceutical companies were faced with the challenge to meet the demand for insulin with the highest possible degree of purity in the required quantities from animal sources. The observatio
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::76cf1bf273d1cc6c723ea749db8e4253
https://doi.org/10.1002/anie.201702493
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9
Preparation of Selenoinsulin as a Long‐Lasting Insulin Analogue
Autor: Luis Moroder, Yuya Asahina, Kenta Arai, Toshiki Takei, Masaki Okumura, Satoshi Watanabe, Kenji Inaba, Yuta Amagai, Michio Iwaoka, Hironobu Hojo
Publikováno v: Angewandte Chemie International Edition. 56:5522-5526
Synthetic insulin analogues with a long lifetime are current drug targets for the therapy of diabetic patients. The replacement of the interchain disulfide with a diselenide bridge, which is more resistant to reduction and internal bond rotation, can
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8fafea394259bd0012465cf8cd0ade4f
https://doi.org/10.1002/anie.201701654
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10
Characterization and optimization of two-chain folding pathways of insulin via native chain assembly
Autor: Kenji Inaba, Hidekazu Katayama, Shouta Fujisawa, Reina Shinozaki, Setsuko Ando, Toshiki Takei, Masato Noguchi, Hironobu Hojo, Luis Moroder, Michio Iwaoka, Kenta Arai, Masaki Okumura
Publikováno v: Communications Chemistry
Communications Chemistry, Vol 1, Iss 1, Pp 1-11 (2018)
Until recently the total synthesis of insulin, with its characteristic heterodimeric structure crosslinked by two interchain and one intrachain disulfide (SS) bridge, remained largely an unsolved challenge. By optimizing the synthesis and directed di
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::494d852b6071ab6dcfd3f35497602b7d
https://hdl.handle.net/21.11116/0000-0002-A4BB-221.11116/0000-0002-A4BD-0
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