Zobrazeno 1 - 10
of 34
pro vyhledávání: '"John J. Portman"'
Autor:
Sajad Shiekh, Golam Mustafa, Sineth G. Kodikara, Mohammed Enamul Hoque, Eric Yokie, John J. Portman, Hamza Balci
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 119(30)
We present single molecule experimental and computational modeling studies investigating the accessibility of human telomeric overhangs of physiologically relevant lengths. We studied 25 different overhangs that contain 4-28 repeats of GGGTTA (G-Trac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e2e85d43906a47783311278f88a11a5c
https://pubmed.ncbi.nlm.nih.gov/36070346
https://pubmed.ncbi.nlm.nih.gov/36070346
Publikováno v:
Biophysical Journal. 121:67a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0b6e4d8098e7b3aa63b287d8e37be183
https://doi.org/10.1016/j.bpj.2021.11.2402
https://doi.org/10.1016/j.bpj.2021.11.2402
Autor:
John J. Portman, Swarnendu Tripathi
Publikováno v:
The Journal of Physical Chemistry B. 117:13182-13193
The N-terminal receiver domain of protein NtrC (NtrC(r)) exhibits allosteric transitions between the inactive (unphosphorylated) and active (phosphorylated) state on the microsecond time scale. Using a coarse-grained variational model with coupled en
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b6ec562455f9a5d79fb4b351e319878c
https://doi.org/10.1021/jp403181p
https://doi.org/10.1021/jp403181p
Autor:
John J. Portman, Prithviraj Nandigrami
Publikováno v:
The Journal of chemical physics. 144(10)
Interactions between a protein and a ligand are often accompanied by a redistribution of the population of thermally accessible conformations. This dynamic response of the protein's functional energy landscape enables a protein to modulate binding af
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e604b34cccf75a045137df53ccc3528e
https://pubmed.ncbi.nlm.nih.gov/26979705
https://pubmed.ncbi.nlm.nih.gov/26979705
Autor:
Prithviraj Nandigrami, John J. Portman
Publikováno v:
The Journal of chemical physics. 144(10)
Calmodulin (CaM) is a ubiquitous calcium binding protein consisting of two structurally similar domains with distinct stabilities, binding affinities, and flexibilities. We present coarse grained simulations that suggest the mechanism for the domain'
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3b847aafb5ad565e9ae76d9ab00331d6
https://pubmed.ncbi.nlm.nih.gov/26979706
https://pubmed.ncbi.nlm.nih.gov/26979706
Autor:
Prithviraj Nandigrami, John J. Portman
Publikováno v:
Biophysical Journal. 110(3)
Calmodulin (CaM) is a well-characterized calcium binding protein that undergoes allosteric transition between closed and open conformations upon binding two calcium ions to each of its two domains. Such conformational transition upon binding provides
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d75d3e9341744309afd9894adf1be69
Autor:
Daniel Gavazzi, John J. Portman
Publikováno v:
Biophysical Journal. 112:497a-498a
Although the three domains of α-spectrin (R15, R16, and R17) are highly homologous, experiments reveal striking differences in their folding mechanism and kinetics. In particular, the R15 domain's folding rate is measured to be three orders of magni
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4cf09244f71040f56432f12ff0b931d2
https://doi.org/10.1016/j.bpj.2016.11.2691
https://doi.org/10.1016/j.bpj.2016.11.2691
Autor:
John J. Portman
Publikováno v:
Current Opinion in Structural Biology. 20:11-15
Despite the large and complex conformational space available to an unfolded protein, many small globular proteins fold with simple two-state cooperative kinetics. Understanding what determines folding rates beyond simple rules summarizing kinetic tre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::12316ecc39a3cd0d2ea46c04960e4eca
https://doi.org/10.1016/j.sbi.2009.12.013
https://doi.org/10.1016/j.sbi.2009.12.013
Autor:
John J. Portman, Xianghong Qi
Publikováno v:
Proceedings of the National Academy of Sciences. 104:10841-10846
A coarse-grained variational model is used to investigate the polymer dynamics of barrier crossing for a diverse set of two-state folding proteins. The model gives reliable folding rate predictions provided excluded volume terms that induce minor str
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e2ac8715b362e2c21eb86660ada1c243
https://doi.org/10.1073/pnas.0609321104
https://doi.org/10.1073/pnas.0609321104
Autor:
John J. Portman, Hugh Nymeyer, Angel E. Garcia, Kevin Y. Sanbonmatsu, Sandrasegaram Gnanakaran
Publikováno v:
Current Opinion in Structural Biology. 13:168-174
Developments in the design of small peptides that mimic proteins in complexity, recent advances in nanosecond time-resolved spectroscopy methods to study peptides and the development of modern, highly parallel simulation algorithms have come together
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bb21bf9ad086f511d489aa2a0dc75bd4
https://doi.org/10.1016/s0959-440x(03)00040-x
https://doi.org/10.1016/s0959-440x(03)00040-x