Results 181 to 190 of about 795,036 (219)
Shy is a proteobacterial steroid hydratase which catalyzes steroid side chain degradation without requiring a catalytically inert partner domain. [PDF]
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Side chain‐to‐side chain cyclization by click reaction
Journal of Peptide Science, 2009AbstractCuI‐catalyzed azide‐alkyne 1,3‐dipolar Huisgen's cycloaddition (CuAAC) is a click reaction that has drawn a lot of attention, in general, and in the field of peptide and protein sciences, in particular. Among several reported applications, the preparation of novel heterodetic cyclopeptides by an intramolecular side chain‐to‐side chain CuAAC ...
Alexandra Le Chevalier Isaad +4 more
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The ST pinch: A side chain‐to‐side chain hydrogen‐bonded motif
Proteins: Structure, Function, and Bioinformatics, 2012AbstractThe ST Pinch is a 12‐membered hydrogen‐bonded motif (Ser/Thr‐Xaa‐Ser/Thr) involving the side chain oxygen atoms of two Ser/Thr residues. We identified the ST Pinch in 104 proteins in a database containing high‐resolution crystal structures. Conformational analysis of the ST Pinch in these proteins points to specific preferences for the Xaa ...
Martha G. Bomar +4 more
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Addition of side chains to a known backbone with defined side-chain centroids
Biophysical Chemistry, 2002An automatic procedure is proposed for adding side chains to a protein backbone; it is based on optimization of a simplified energy function for peptide side chains, given its backbone and positions of side-chain centroids. The energy is expressed as a sum of the energies of interaction between side chains, and a harmonic penalty function accounting ...
Rajmund Kaźmierkiewicz +3 more
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Stable helical peptoids via covalent side chain to side chain cyclization [PDF]
Organic & Biomolecular Chemistry, 2008 Peptoids are oligomeric N-substituted glycines with potential as biologically relevant compounds. Helical peptoids provide an attractive fold for the generation of protein-protein interaction inhibitors. The generation of helical peptoid folds in organic and aqueous media has been limited to strict design rules, as peptoid-folding is mainly directed ...
Belen Vaz, Luc Brunsveld
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Degradation of the lanosterol side-chain
Tetrahedron Letters, 19703β-Acetoxylanosta-8,24-diene (1) has been converted by a six-step degradation into 3β-acetoxy-4,4,14α-tri-methyl-5α-pregn-8-en-2-one (14).
Peter S. Rutledge +2 more
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Side-chain–side-chain interactions and stability of the helical state
Physical Review E, 2014Understanding the driving forces that lead to the stability of the secondary motifs found in proteins, namely α-helix and β-sheet, is a major goal in structural biology. The thermodynamic stability of these repetitive units is a result of a delicate balance between many factors, which in addition to the peptide chain involves also the solvent.
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Phytosterol side chain biosynthesis
Lipids, 1974AbstractThe typical plant sterols contain a substituent at C‐24 of the side chain. This can be a methylene, ethylidene, methyl, or ethyl group; with the last three groups, all possible isomers have been reported in nature. The C‐24 alkyl groups are derived by a transmethylation reaction from methionine.
John R. Lenton +3 more
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The influence of the side chain on sterol side-chain cleavage in rat adrenal glands
Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1982The cholesterol side-chain cleavage enzyme system of rat adrenal cortex, the enzyme catalyzing a rate-limiting step of adrenal steroidogenesis, was shown to metabolize a series of cholesterol analogues to pregnenolone. In the presence of Ca2+, rat adrenocortical mitochondria converted the analogue with two less methylene groups (C25) than cholesterol ...
Iain F. Craig +3 more
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