Zobrazeno 1 - 10
of 183
pro vyhledávání: '"R.E. Dickerson"'
Publikováno v:
Journal of Biological Chemistry. 266:8861-8883
Publikováno v:
Acta Crystallographica Section A Foundations of Crystallography. 52:C154-C155
Publikováno v:
Radiotherapy and Oncology. 40:S89
Publikováno v:
Acta Crystallographica Section B Structural Science. 41:255-262
A structure-factor least-squares refinement of the deoxyoligonucleotide (CGCGAATTCGCG)2 has been conducted using a model with constraints and restraints on the positional parameters and a segmented rigid-body representation for the anisotropic temper
Autor:
H.R. Drew, R.E. Dickerson
Publikováno v:
The EMBO journal. 1(6)
DNA polymers containing exclusively A.T or I.C base pairs frequently exhibit D- or E-type X-ray diffraction patterns when dried. The distribution of intensities in fiber patterns appears to demand helical structures with 7 and 7.5 bp/turn, respective
Publikováno v:
Cold Spring Harbor symposia on quantitative biology.
Autor:
R.E. Dickerson
Publikováno v:
Biomolecular Structure, Conformation, Function, and Evolution
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::36894f3e9cf095d15b26ebae5ff5e07b
https://doi.org/10.1016/b978-1-4832-8364-7.50022-2
https://doi.org/10.1016/b978-1-4832-8364-7.50022-2
Publisher Summary This chapter focuses on functional limits of cytochrome c variability. Cytochrome c is the protein for which the primary structure is known for the largest number of species and covering the complete taxonomic scale. Though some sev
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4c8075385d588c9590da20a937b6666f
https://doi.org/10.1016/b978-0-08-016874-6.50007-2
https://doi.org/10.1016/b978-0-08-016874-6.50007-2
Publikováno v:
Journal of molecular biology. 50(1)
The structure of the tetragonal form of lysozyme has been established and X-ray diffraction data have been measured for the triclinic form. The rotation function of Rossmann & Blow (1962) has been used to determine the orientation of the lysozyme mol