Zobrazeno 1 - 10
of 31
pro vyhledávání: '"Diana E. Schlamadinger"'
Autor:
Sunil Kumar, Melissa Birol, Diana E. Schlamadinger, Slawomir P. Wojcik, Elizabeth Rhoades, Andrew D. Miranker
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-11 (2016)
Intrinsically disordered proteins that form amyloid fibrils are hard to target with traditional therapeutic approaches. Here, the authors report on an oligoquinoline derivative that binds the human islet amyloid polypeptide, stabilising an alpha-heli
Externí odkaz:
https://doaj.org/article/665697c8a506443f9f23cfe44a5d3983
Autor:
James A. Hebda, Sunil Kumar, Andrew D. Hamilton, Elizabeth Rhoades, Diana E. Schlamadinger, Brandon Q. Mercado, Joanna M. Dunn, Ishu Saraogi, Mark A. Brown, Andrew D. Miranker
Publikováno v:
Chemistry & Biology. 22(3):369-378
SummaryIslet amyloid polypeptide (IAPP) is a hormone cosecreted with insulin. IAPP proceeds through a series of conformational changes from random coil to β-sheet via transient α-helical intermediates. An unknown subset of these events are associat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6fda20216ee806b4ba47f5365fdb0c4d
Publikováno v:
Biochemistry
Homomeric self-assembly of peptides into amyloid fibers is a feature of many diseases. A central role has been suggested for the lateral fiber surface affecting gains of toxic function. To investigate this, a protein scaffold that presents a discrete
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::49e579ea387828573b13bd3f0e451a93
http://europepmc.org/articles/PMC4318585
http://europepmc.org/articles/PMC4318585
Publikováno v:
Protein Science. 22:870-882
Three families of membrane-active peptides are commonly found in nature and are classified according to their initial apparent activity. Antimicrobial peptides are ancient components of the innate immune system and typically act by disruption of micr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2da6ff7bf25bd0794e9ce8d0c2220c9a
https://doi.org/10.1002/pro.2274
https://doi.org/10.1002/pro.2274
Autor:
Diana E. Schlamadinger, Melissa Birol, Sunil Kumar, Andrew D. Miranker, Elizabeth Rhoades, Slawomir P. Wojcik
Publikováno v:
Nature Communications
Nature Communications, Vol 7, Iss 1, Pp 1-11 (2016)
Nature Communications, Vol 7, Iss 1, Pp 1-11 (2016)
Disordered proteins, such as those central to Alzheimer's and Parkinson's, are particularly intractable for structure-targeted therapeutic design. Here we demonstrate the capacity of a synthetic foldamer to capture structure in a disease relevant pep
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::31fad488fef84cbbd2c8010bd29068cc
https://doi.org/10.1038/ncomms11412
https://doi.org/10.1038/ncomms11412
Publikováno v:
Journal of Raman Spectroscopy. 43:1459-1464
Aromatic interactions are important stabilizing forces in proteins but are difficult to detect in the absence of high-resolution structures. Ultraviolet resonance Raman spectroscopy is used to probe the vibrational signatures of aromatic interactions
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8593d14c0f64e41396dacfe5119470f9
https://doi.org/10.1002/jrs.4061
https://doi.org/10.1002/jrs.4061
Publikováno v:
Journal of Chemical Education. 87:961-964
Laboratory experiments that focus on protein folding provide excellent opportunities for undergraduate students to learn important topics in the expanding interdisciplinary field of biophysics. Here, we describe the use of Stern−Volmer plots to det
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9b92a00e4354d31c8e5d4fbce3e472b8
https://doi.org/10.1021/ed900029c
https://doi.org/10.1021/ed900029c
Publikováno v:
Biochemistry. 47:12844-12852
Refolding curves of the integral membrane protein outer membrane protein A (OmpA) were measured to determine the conformational stabilities of this model system for membrane protein folding. Wild-type OmpA exhibits a free energy of unfolding (DeltaG
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fc39ea3e5d1b1e88c07538d3b489478a
https://doi.org/10.1021/bi800860k
https://doi.org/10.1021/bi800860k
Insights into Protein Structure and Dynamics by Ultraviolet and Visible Resonance Raman Spectroscopy
Publikováno v:
Biochemistry. 54(31)
Raman spectroscopy is a form of vibrational spectroscopy based on inelastic scattering of light. In resonance Raman spectroscopy, the wavelength of the incident light falls within an absorption band of a chromophore, and this overlap of excitation an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b1b507ef6ccebf91e2b21ae99ba64c58
https://pubmed.ncbi.nlm.nih.gov/26219819
https://pubmed.ncbi.nlm.nih.gov/26219819
Publikováno v:
Biochemistry. 54(22)
Islet amyloid polypeptide (IAPP) is a peptide hormone whose pathological self-assembly is a hallmark of the progression of type II diabetes. IAPP–membrane interactions catalyze its higher-order self-assembly and also underlie its toxic effects towa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0b4e59597b0bbd2e6e2ac61ca73ffd10
https://pubmed.ncbi.nlm.nih.gov/25966003
https://pubmed.ncbi.nlm.nih.gov/25966003