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The ability to design efficient enzymes from scratch would have a profound effect on chemistry, biotechnology and medicine. Rapid progress in protein engineering over the past decade makes us optimistic that this ambition is within reach. The development of artificial enzymes containing metal cofactors ...
An essential protein of the SARS-CoV-2 virus, the envelope protein E, forms a homopentameric cation channel that is important for virus pathogenicity. Here we report a 2.1-Å structure and the drug-binding site of E’s transmembrane domain (ETM), determined using solid-state NMR spectroscop...
Design of a heme-binding four-helix bundle J. Am. Chem. Soc, 116 (1994), pp. 856-865 CrossrefView in ScopusGoogle Scholar [5] T.P Quinn, N.B Tweedy, R.W Williams, J.S Richardson, D.C Richardson Betadoublet: de novo design, synthesis and characterization of a β-sandwich protei...
Overall this work presents the design and synthesis of four-helix bundles containing peptides with and without N- and C-glycine caps. It was predicted that, if the glycine caps were indeed responsible for holding the tertiary structures intact, the caviteins lacking glycine capping residues would...
The GRAS gene family in ArabidopsisArabidopsis sequence characterization and basic expression analysis of the 热度: characterization by 16s rrna sequence analysis of pseudomonads 热度: De Novo Design Expression and Characterization of Felix:A Four-Helix Bundle Protein of Native-Like Sequence 热度: ...
The CWxP motif of transmembrane helix 6 (x: any residue) is highly conserved in class A GPCRs. Within this motif, W6.48 is a big star in the theory of the global “toggle switch” because of its key role in the activation mechanism of GPCRs upon ligand b
Little was known about the predicted TM portion of FlhB/SctU. Co-evolution analysis and molecular modelling led to suggestions that it forms a four-helix bundle in the membrane18, whereas crosslinks19 and partial co-purification of FlhB with FliPQR were consistent with FlhB/SctU interacting wit...
From the crystal structure of the related Max/Max homodimer, it is to be assumed that the Myc/Max dimer forms a parallel, left-handed, four-helix bundle, with each monomer containing two a-helical segments separated by a loop. While the basic region and the N-terminal helices mediate ...