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Spontaneous assembly of a self-complementary oligopeptide to form a stable macroscopic membrane.
- S. Zhang, T. Holmes, C. Lockshin, A. Rich
- BiologyProceedings of the National Academy of Sciences…
- 15 April 1993
This work has shown that a 16-residue peptide has a characteristic beta-sheet circular dichroism spectrum in water and spontaneously assembles to form a macroscopic membrane, which may be a model for studying the insoluble peptides found in certain neurological disorders.
Widespread A-to-I RNA Editing of Alu-Containing mRNAs in the Human Transcriptome
Intramolecular pairs of Alu elements are identified as a major target for editing in the human transcriptome and it is suggested that modification of repetitive elements is a predominant activity for RNA editing with significant implications for cellular gene expression.
Molecular structure of a left-handed double helical DNA fragment at atomic resolution
The DNA fragment d(CpGpCpGpCpG) crystallises as a left-handed double helical molecule with Watson–Crick base pairs and an antiparallel organisation of the sugar phosphate chains. The helix has two…
Sequence-specific recognition of double helical nucleic acids by proteins.
- N. Seeman, J. Rosenberg, A. Rich
- Biology, PhysicsProceedings of the National Academy of Sciences…
- 1 March 1976
It is concluded that a single hydrogen bond is inadequate for uniquely identifying any particular base pair, as this leads to numerous degeneracies, but using two hydrogen bonds, fidelity of base pair recognition may be achieved.
Structure of the DLM-1–Z-DNA complex reveals a conserved family of Z-DNA-binding proteins
- T. Schwartz, J. Behlke, K. Lowenhaupt, U. Heinemann, A. Rich
- Biology, ChemistryNature Structural Biology
- 1 November 2018
It is found that the tumor-associated protein DLM-1 contains a domain with remarkable sequence similarities to ZαADAR, suggesting the existence of a family of winged-helix proteins sharing a common Z-DNA binding motif.
Extensive neurite outgrowth and active synapse formation on self-assembling peptide scaffolds.
- T. Holmes, S. de Lacalle, X. Su, G. Liu, A. Rich, S. Zhang
- Biology, ChemistryProceedings of the National Academy of Sciences…
- 6 June 2000
A new type of self-assembling peptide (sapeptide) scaffolds that serve as substrates for neurite outgrowth and synapse formation is described, and they did not elicit a measurable immune response or tissue inflammation when introduced into animals.
Structural domains of transfer RNA molecules.
Various detailed features of the conformation of yeast tRNA(Phe) revealed by recent refinement analysis of x-ray diffraction data at 2.5 A resolution are described.
Crystal structure of the Zalpha domain of the human editing enzyme ADAR1 bound to left-handed Z-DNA.
The editing enzyme double-stranded RNA adenosine deaminase includes a DNA binding domain, Zalpha, which is specific for left-handed Z- DNA, and the helix-turn-helix motif, frequently used to recognize B-DNA, is used by Zalpha to contact Z-DNA.
Minor groove RNA triplex in the crystal structure of a ribosomal frameshifting viral pseudoknot
The crystal structure of the beet western yellow virus pseudoknot reveals rotation and a bend at the junction of the two stems, which will aid mechanistic analyses of ribosomal frameshifting.