Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Katheryn M Sanchez"'
Autor:
Anna L Cogen, Kenshi Yamasaki, Jun Muto, Katheryn M Sanchez, Laura Crotty Alexander, Jackelyn Tanios, Yuping Lai, Judy E Kim, Victor Nizet, Richard L Gallo
Publikováno v:
PLoS ONE, Vol 5, Iss 1, p e8557 (2010)
Antimicrobial peptides play an important role in host defense against pathogens. Recently, phenol-soluble modulins (PSMs) from Staphylococcus epidermidis (S. epidermidis) were shown to interact with lipid membranes, form complexes, and exert antimicr
Externí odkaz:
https://doaj.org/article/bb9143ba02f24f73a030a2a165940046
Publikováno v:
Biophysical Journal. 100:2121-2130
Aromatic amino acids of membrane proteins are enriched at the lipid-water interface. The role of tryptophan on the folding and stability of an integral membrane protein is investigated with ultraviolet resonance Raman and fluorescence spectroscopy. W
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::19e55ab8d8c924af69a08ae3d28b9f71
https://doi.org/10.1016/j.bpj.2011.03.018
https://doi.org/10.1016/j.bpj.2011.03.018
Publikováno v:
Journal of Raman Spectroscopy. 40:1060-1064
The partitioning of a hydrophobic hexapeptide, N-acetyl-tryptophan-pentaleucine (AcWL5), into self-associated β-sheets within a vesicle membrane was studied as a model for integral membrane protein folding and insertion via vibrational and electroni
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e2ca2f828e8674ce9bfec48e5d212ed6
https://doi.org/10.1002/jrs.2237
https://doi.org/10.1002/jrs.2237
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
Publikováno v:
The Journal of Physical Chemistry B. 112:9507-9511
The vibrational structure of native anchoring tryptophan (Trp) and tyrosine residues in an integral membrane protein, bacterial outer membrane protein A (OmpA), have been investigated using UV resonance Raman (UVRR) spectroscopy for the first time. S
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::32ba20299843b89180adfa44f82dcab0
https://doi.org/10.1021/jp800772j
https://doi.org/10.1021/jp800772j
Autor:
Judy E. Kim, Justin W. Torpey, Katheryn M. Sanchez, Kenshi Yamasaki, Robert A. Dorschner, Victor Nizet, Daniel T. MacLeod, Anna L. Cogen, Michael Otto, Richard L. Gallo, Yuping Lai
Antimicrobial peptides serve as a first line of innate immune defense against invading organisms such as bacteria and viruses. In this study, we hypothesized that peptides produced by a normal microbial resident of human skin, Staphylococcus epidermi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::182f50232e9b643e6e34a0127863fe92
https://europepmc.org/articles/PMC2796468/
https://europepmc.org/articles/PMC2796468/
Autor:
Kenshi Yamasaki, Katheryn M. Sanchez, Richard L. Gallo, Laura E. Crotty Alexander, Jun Muto, Victor Nizet, Jackelyn Tanios, Judy E. Kim, Anna L. Cogen, Yuping Lai
Publikováno v:
PLoS ONE
PLoS ONE, Vol 5, Iss 1, p e8557 (2010)
PLoS ONE, Vol 5, Iss 1, p e8557 (2010)
Antimicrobial peptides play an important role in host defense against pathogens. Recently, phenol-soluble modulins (PSMs) from Staphylococcus epidermidis (S. epidermidis) were shown to interact with lipid membranes, form complexes, and exert antimicr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f8df0c4f8d2a1e5542a914cb4c2448cd
http://europepmc.org/articles/PMC2796718
http://europepmc.org/articles/PMC2796718
Autor:
Diana E. Schlamadinger, Hannah S. Shafaat, Katheryn M. Sanchez, Jonathan E. Gable, Judy E. Kim, P. M. Champion, L. D. Ziegler
Publikováno v:
AIP Conference Proceedings.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2aeaf4110f80ecc856f54fd4aebe0dcb
https://doi.org/10.1063/1.3482447
https://doi.org/10.1063/1.3482447
Publikováno v:
Journal of chemical education. 85(9)
Protein folding is an exploding area of research in biophysics and physical chemistry. Here, we describe the integration of several techniques, including absorption spectroscopy, fluorescence spectroscopy, and Förster resonance energy transfer (FRET
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4efaeff77373ef47e4a10ed960bcc528
https://pubmed.ncbi.nlm.nih.gov/19756254
https://pubmed.ncbi.nlm.nih.gov/19756254
Publikováno v:
Journal of Physical Chemistry B; Jul2008, Vol. 112 Issue 31, p9507-9511, 5p