| Literature DB >> 2987935 |
S Vijay-Kumar, C E Bugg, K D Wilkinson, W J Cook.
Abstract
The three-dimensional structure of ubiquitin has been determined at 2.8 A resolution. X-ray diffraction data for the native protein and derivatives were collected with an automated diffractometer. Phases were obtained by use of a single isomorphous mercuric acetate derivative. The molecule contains a pronounced hydrophobic core. Prominent secondary structural features include three and one-half turns of alpha-helix, a mixed beta-sheet that contains four strands, and seven reverse turns. The histidine, tyrosine, and two phenylalanine residues are located on the surface of the molecule.Entities:
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Year: 1985 PMID: 2987935 PMCID: PMC397829 DOI: 10.1073/pnas.82.11.3582
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN: 0027-8424 Impact factor: 11.205