Zobrazeno 1 - 10
of 73
pro vyhledávání: '"A. T. Whitten"'
Publikováno v:
Molecules, Vol 26, Iss 3, p 634 (2021)
The α and polyproline II (PPII) basins are the two most populated regions of the Ramachandran map when constructed from the protein coil library, a widely used denatured state model built from the segments of irregular structure found in the Protein
Externí odkaz:
https://doaj.org/article/e14f633a034e4867bafd965c1805aab5
Publikováno v:
bioRxiv
Staphylococcus epidermidisandS. aureusare highly problematic bacteria in hospital settings. This stems, at least in part, from strong abilities to form biofilms on abiotic or biotic surfaces. Biofilms are well-organized multicellular aggregates of ba
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d84f2842fdf2c95aeef5661f0315611
https://doi.org/10.1101/2023.01.06.523059
https://doi.org/10.1101/2023.01.06.523059
Autor:
Ayyam Y. Ibrahim, Nathan P. Khaodeuanepheng, Dhanush L. Amarasekara, John J. Correia, Karen A. Lewis, Nicholas C. Fitzkee, Loren E. Hough, Steven T. Whitten
Protein phase separation is thought to be a primary driving force for the formation of membraneless organelles, which control a wide range of biological functions from stress response to ribosome biogenesis. Among phase-separating (PS) proteins, many
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::587278a09305894c420cf38576276f11
https://doi.org/10.1101/2022.08.04.502866
https://doi.org/10.1101/2022.08.04.502866
Publikováno v:
PLoS Computational Biology, Vol 12, Iss 1, p e1004686 (2016)
The properties of disordered proteins are thought to depend on intrinsic conformational propensities for polyproline II (PPII) structure. While intrinsic PPII propensities have been measured for the common biological amino acids in short peptides, th
Externí odkaz:
https://doaj.org/article/9151bbff36024665b0150afb57ba1b8c
Autor:
Erin C. Tilton, Elisia A. Paiz, George L. Parra, Steven T. Whitten, Sarah M. Voss, Stephen So, Lance R. English
Publikováno v:
J Phys Chem B
Conformational equilibria in the protein denatured state have key roles regulating folding, stability, and function. The extent of conformational bias in the protein denatured state under folding conditions, however, has thus far proven elusive to qu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2b24484e9228e255bc229d608d98e708
https://doi.org/10.1021/acs.jpcb.9b09088
https://doi.org/10.1021/acs.jpcb.9b09088
Publikováno v:
The FASEB Journal. 35
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8258cc45dc315a3d4ed7e83f909529ac
https://doi.org/10.1096/fasebj.2021.35.s1.04916
https://doi.org/10.1096/fasebj.2021.35.s1.04916
Autor:
John J. Correia, Nicholas C. Fitzkee, Elisia A. Paiz, Loren E. Hough, Jeffre H. Allen, Steven T. Whitten
The complex cellular milieu can spontaneously de-mix in a process controlled in part by proteins that are intrinsically disordered (ID). A protein’s propensity to de-mix is thought to be driven by the preference for protein-protein rather than prot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::893589234bddaaa2a60828d498407908
https://doi.org/10.1101/2020.07.06.189613
https://doi.org/10.1101/2020.07.06.189613
Publikováno v:
Biophysical Journal. 115:328-340
Sequence patterns of charge, hydrophobicity, hydrogen bonding, and other amino acid physicochemical properties contribute to mechanisms of protein folding, but how sequence composition and patterns influence the conformational dynamics of the denatur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5efdbfc6081bdb97ea16c3d1794ca054
https://doi.org/10.1016/j.bpj.2018.06.006
https://doi.org/10.1016/j.bpj.2018.06.006
Autor:
Nicholas C. Fitzkee, Elisia A. Paiz, John J. Correia, Jeffre H. Allen, Loren E. Hough, Steven T. Whitten
Publikováno v:
The Journal of Biological Chemistry
The complex cellular milieu can spontaneously demix, or phase separate, in a process controlled in part by intrinsically disordered (ID) proteins. A protein's propensity to phase separate is thought to be driven by a preference for protein–protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::883efbb92e2e157405838e8c563ed1cb
https://doi.org/10.1016/j.jbc.2021.101343
https://doi.org/10.1016/j.jbc.2021.101343
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 85:296-311
Proteins that lack tertiary stability under normal conditions, known as intrinsically disordered, exhibit a wide range of biological activities. Molecular descriptions for the biology of intrinsically disordered proteins (IDPs) consequently rely on d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3163fe527ffeddb4d6e88701661c8812
https://doi.org/10.1002/prot.25222
https://doi.org/10.1002/prot.25222