Zobrazeno 1 - 10
of 24
pro vyhledávání: '"D. Sneden"'
Autor:
Alexander Rich, D. Sneden, Sung-Hou Kim, J. J. Kim, F. L. Suddath, A. McPherson, Gary J. Quigley
Publikováno v:
Nature. 248:20-24
At 3A resolution, the electron density map of crystalline tRNA shows the polynucleotide chain as an alternating series of ribose and phosphate peaks. Bases are seen, especially in the double helical stem regions. A complete three-dimensional model of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::100679f66f029ccc0db786d7f55dde41
https://doi.org/10.1038/248020a0
https://doi.org/10.1038/248020a0
Autor:
D. Sneden, A. McPherson, P. Blattmann, Sung-Hou Kim, Alexander Rich, F. L. Suddath, J. Weinzierl, Gary J. Quigley, J. J. Kim
Publikováno v:
Proceedings of the National Academy of Sciences. 69:3746-3750
Three isomorphous heavy-atom derivatives have been obtained of orthorhombic crystals of phenylalanine transfer RNA from yeast. These derivatives contain osmium, samarium, and platinum. The positions of the heavy atoms have been determined; these have
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c1a43878b74105c14c02e0b87f04832
https://doi.org/10.1073/pnas.69.12.3746
https://doi.org/10.1073/pnas.69.12.3746
Autor:
J. Weinzierl, F. L. Suddath, A. McPherson, Alexander Rich, Gary J. Quigley, D. Sneden, J. J. Kim, Sung-Hou Kim
Publikováno v:
Journal of Molecular Biology. 75:429-432
The orthorhombic unit cell of crystalline yeast phenylalanine transfer RNA has dimensions a = 33 A , b = 56 A and c = 161 A . When the mother liquor dries partially, a series of transformations takes place in which the a and b axes change very little
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ee5ac659eee667683da866a07ca8ea66
https://doi.org/10.1016/0022-2836(73)90032-6
https://doi.org/10.1016/0022-2836(73)90032-6
Three-Dimensional Structure of Yeast Phenylalanine Transfer RNA: Folding of the Polynucleotide Chain
Autor:
J. J. Kim, Sung-Hou Kim, A. McPherson, Gary J. Quigley, J. Weinzierl, F. L. Suddath, Alexander Rich, D. Sneden
Publikováno v:
Science. 179:285-288
At 4 A resolution the polynucleotides in yeast phenylalanine transfer RNA are seen in a series of electron dense masses about 5.8 A apart. These peaks are probably associated with the phosphate groups, while lower levels of electron density between s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e35b2950431730e2249bd8edebf9c4ba
https://doi.org/10.1126/science.179.4070.285
https://doi.org/10.1126/science.179.4070.285
The molecular structure of monoclinic crystals of yeast phenylalanine tRNA is analyzed by comparing it to the orthorhombic crystals of the same material whose structure has been determined. Changing the packing of the molecule from the head-to-head,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ca7ea70fe7097ef4d7ff0ac1cf776824
https://europepmc.org/articles/PMC388404/
https://europepmc.org/articles/PMC388404/
Autor:
Sung-Hou Kim, J. Weinzierl, Alexander Rich, A. McPherson, F. L. Suddath, J. J. Kim, Gary J. Quigley, D. Sneden
Publikováno v:
Journal of molecular biology. 75(2)
Yeast phenylalanine transfer RNA has been found to crystallize in five different crystal systems involving eight different space groups. The X-ray diffraction characteristics of these forms are described. One of the orthorhombic forms yields a diffra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6df1b82eec079c8484016d1cdc470467
https://pubmed.ncbi.nlm.nih.gov/4580683
https://pubmed.ncbi.nlm.nih.gov/4580683
Publikováno v:
Nature. 241:530-531
DURING protein synthesis in bacteria, aminoacyl tRNA is transported to the ribosome complexed with a protein elongation factor Tu (EF-TU) and GTP1–3. In the ribosome the aminoacyl tRNA is positioned onto its appropriate codon, GTP is hydrolysed, an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::997e35515e6a5d6f8f049f46cbb79393
https://doi.org/10.1038/241530a0
https://doi.org/10.1038/241530a0
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