Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Michelle R. Bunagan"'
Autor:
Michelle R. Bunagan, Rebecca M. Triano, Levi A. Ekanger, Rebecca A. Hunter, J. Lynn Gazley, Abby R. O’Connor, Joseph L. Baker, Benny C. Chan
Publikováno v:
Journal of Chemical Education
The College of New Jersey’s Chemistry Department and School of Science have been strategically transforming our teaching, learning, and mentoring environments for over a decade through programs tha...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff59b9b588498d4097b4e3e5728ce69a
Publikováno v:
Journal of Peptide Science. 26
The effect of choline chloride on the conformational dynamics of the 11-mer repeat unit P1LEA-22 of group 3 Late Embryogenesis Abundant (G3LEA) proteins was studied. Circular dichroism data of aqueous solutions of P1LEA-22 revealed that the peptide f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ddb1360fd9762bd925fc1beaf552d98c
https://doi.org/10.1002/psc.3247
https://doi.org/10.1002/psc.3247
Publikováno v:
Biophysical Journal. 118:354a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::abf401acabde649323241ce8f3c441d9
https://doi.org/10.1016/j.bpj.2019.11.2040
https://doi.org/10.1016/j.bpj.2019.11.2040
Publikováno v:
Biophysical Journal. 118:357a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a479f1baf5090236b52cce3fa2c72ba8
https://doi.org/10.1016/j.bpj.2019.11.2056
https://doi.org/10.1016/j.bpj.2019.11.2056
Publikováno v:
Angewandte Chemie. 123:11076-11079
Protein folding kinetics are often measured by monitoring the change of a single spectroscopic signal, such as the fluorescence of an intrinsic fluorophore or the absorbance at a single frequency within an electronic or vibrational band of the protei
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::86b90133bd0c63793d1103ff21e185b0
https://doi.org/10.1002/ange.201104085
https://doi.org/10.1002/ange.201104085
Publikováno v:
Journal of the American Chemical Society. 131:7470-7476
Backbone-backbone hydrogen bonds are a common feature of native protein structures, yet their thermodynamic and kinetic influence on folding has long been debated. This is reflected by the disparity between current protein folding models, which place
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e8faa739a4a1aa2176fcb7b21db3a16e
https://doi.org/10.1021/ja901860f
https://doi.org/10.1021/ja901860f
Publikováno v:
Biophysical Journal. 93:4076-4082
The formation of the monomeric alpha-helix represents one of the simplest scenarios in protein folding; however, our current understanding of the folding dynamics of the alpha-helix motif is mainly based on studies of alanine-rich model peptides. To
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::501e6afd6eebb134788df61819c7fefd
https://doi.org/10.1529/biophysj.107.108548
https://doi.org/10.1529/biophysj.107.108548
Publikováno v:
Protein Science. 16:1176-1183
Small proteins often fold in an apparent two-state manner with the absence of detectable early-folding intermediates. Recently, using native-state hydrogen exchange, intermediates that exist after the rate-limiting transition state have been identifi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e67f10daa1857f7faa7692e05d89e5ca
https://doi.org/10.1110/ps.062505607
https://doi.org/10.1110/ps.062505607
Publikováno v:
The Journal of Physical Chemistry B. 110:3759-3763
Miniproteins provide useful model systems for understanding the principles of protein folding and design. These proteins also serve as useful test cases for theories of protein folding, and their small size and ultrafast folding kinetics put them in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0f06491d1baa58499c65d32304879773
https://doi.org/10.1021/jp055288z
https://doi.org/10.1021/jp055288z
Publikováno v:
The Journal of Physical Chemistry B. 109:22273-22284
Aqueous poly(ethylene oxide)-poly(propylene oxide)-poly(ethylene oxide) (PEO109-PPO41-PEO109) copolymers are nonionic surfactants that self-organize to form aggregate structures with increasing temperature or concentration. We have studied two concen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::31e560b8cffe1e90c85b6bd8e395adcf
https://doi.org/10.1021/jp053929k
https://doi.org/10.1021/jp053929k