Zobrazeno 1 - 10
of 11
pro vyhledávání: '"J R, Mourant"'
Publikováno v:
Physical Review Letters. 74:2607-2610
After photodissociation of carbon monoxide bound to myoglobin, a thermally driven conformational relaxation towards the equilibrium structure of the deligated protein occurs above 160 K. Here we show that a relaxation can already be induced at lower
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e3b10b58cc1e7a306556f8ff0724ab0
https://doi.org/10.1103/physrevlett.74.2607
https://doi.org/10.1103/physrevlett.74.2607
Autor:
D. Braunstein, Robert D. Young, Pál Ormos, Hans Frauenfelder, K. Chu, G. U. Nienhaus, J. R. Mourant
Publikováno v:
Scopus-Elsevier
Phenomena occurring in the heme pocket after photolysis of carbonmonoxymyoglobin (MbCO) below about 100 K are investigated using temperature-derivative spectroscopy of the infrared absorption bands of CO. MbCO exists in three conformations (A substra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cce46a5f802647c2762a572ed7b1200d
https://doi.org/10.1016/s0006-3495(93)81218-9
https://doi.org/10.1016/s0006-3495(93)81218-9
Autor:
Icko E T Iben, Lou Reinisch, Pál Ormos, Stan Luck, Robert D. Young, Larry B. Sorensen, Aihua Xie, B. R. Cowen, Hans Frauenfelder, J. Bruce Johnson, M. K. Hong, E. Shyamsunder, Reinhard Scholl, Alfons Schulte, Kwok To Yue, M. C. Marden, Neil A. Alberding, Anjum Ansari, D. Braunstein, Peter J. Steinbach, J. R. Mourant
Publikováno v:
The Journal of Physical Chemistry. 94:1024-1037
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6f9dd148f975c5e23506d192484c9bcd
https://doi.org/10.1021/j100366a002
https://doi.org/10.1021/j100366a002
Publikováno v:
Journal of gravitational physiology : a journal of the International Society for Gravitational Physiology. 6(1)
A small, lightweight system capable of noninvasive measurement of drug concentrations in tissue, without the use of reagents, would be advantageous for the study of the drug pharmacokinetics in space-travel applications. We have applied elastic-scatt
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::cc62867b70b04a78bdcbc9480b25918d
https://pubmed.ncbi.nlm.nih.gov/11543008
https://pubmed.ncbi.nlm.nih.gov/11543008
Publikováno v:
Cancer. 84(6)
The objective of this study was to determine whether there are intrinsic differences in the light scattering properties of tumorigenic and nontumorigenic cells from a multistep carcinogenesis model.Wavelength-dependent and polarization-dependent ligh
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::52c2c552041dd0fb9f2ca0c51b5890bf
https://pubmed.ncbi.nlm.nih.gov/9915139
https://pubmed.ncbi.nlm.nih.gov/9915139
Publikováno v:
Biochemistry. 33(45)
Extended illumination slows the rebinding of CO to myoglobin after photodissociation at cryogenic temperatures. Two types of models have been put forward to explain the effect: motions of the CO within the heme pocket or conformational transitions of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::46a366d199facba9dc87ed0dc4f41644
https://pubmed.ncbi.nlm.nih.gov/7947750
https://pubmed.ncbi.nlm.nih.gov/7947750
Autor:
Robert D. Young, Karen D. Egeberg, Barry A. Springer, Stephen G. Sligar, Hans Frauenfelder, K. Chu, Pál Ormos, G. U. Nienhaus, J. R. Mourant, D. Braunstein
Publikováno v:
Scopus-Elsevier
Fouier-transform infrared (FTIR) difference spectra of several His-E7 and Val-E11 mutants of sperm whale carbonmonoxymyoglobin were obtained by photodissociation at cryogenic temperatures. The IR absorption of the CO ligand shows characteristic featu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::13e1d3f526485fda63e7d04de74e1186
https://pubmed.ncbi.nlm.nih.gov/8312483
https://pubmed.ncbi.nlm.nih.gov/8312483
Publikováno v:
Scopus-Elsevier
Infrared spectroscopy is used to characterize the transitions in the photocycle of bR involving the M intermediate. It has been shown previously that in this part of the photocycle a large protein conformational change takes place that is important f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::883ac681508670605f3f46b21bde6abd
https://pubmed.ncbi.nlm.nih.gov/1637826
https://pubmed.ncbi.nlm.nih.gov/1637826
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 89(7)
The time and temperature dependencies of the line area (M0) and position (M1) of band III at approximately 760 nm have been measured with Fourier-transform infrared spectroscopy in deoxymyoglobin (Mb) and continuously photolyzed carbon monoxide myogl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::edca3b20bcc639d6f17597d5f61136fb
https://pubmed.ncbi.nlm.nih.gov/1557397
https://pubmed.ncbi.nlm.nih.gov/1557397
Autor:
Pál Ormos, B. R. Cowen, Reinhard Scholl, Hans Frauenfelder, D. Braunstein, Alfons Schulte, Peter J. Steinbach, J. R. Mourant, M. K. Hong, Icko Iben
Myoglobin, a simppe dioxygen-storage protein, is a good laboratory for the investigation of the connection between protein structure, dynamics, and function. Fourier-transform infrared spectroscopy on carbon-monoxymyoglobin (MbCO) shows three major C
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::465f0c371ecbfd1bfe1d7406db91d29d
https://europepmc.org/articles/PMC1280983/
https://europepmc.org/articles/PMC1280983/
