Search results for "Sequence"

ChemInform Abstract: Reactions of the Hydrofluoroborate Salts of Open-Chain Analogues of Reissert Compounds with Some α,β-Ethylenic Esters.

2010

The reaction of the hydrofluoroborate salt of an open-chain analogue of a Reissert compound with some α,β-ethylenic esters does not give a [4 + 2] cycloadduct, as previously described in the case of ethyl acrylate. The reaction starts with a 1,3-dipolar cycloaddition of a munchnone imine 5c, d. The [3 + 2] cycloadducts 13 evolve via a rearrangement–condensation sequence to give a substituted 2-pyridone derivative 18 or 19. The proposed mechanism has been verified by the isolation and structural X-ray analysis of some compounds of the reaction sequence.

Chemoenzymatic-Chemical Synthesis of a (2-3)-Sialyl T Threonine Building Block and Its Application to the Synthesis of the N-Terminal Sequence of Leu…

2001

Protection of all functional groups of the carbohydrate portion of the chemoenzymatically synthesized sialyl T threonine ester 1 (R=R1 =H, R2 =tBu, Fmoc=9-fluorenylmethoxycarbonyl) and subsequent acidolysis of the tert-butyl ester afforded the building block 2 (R=Ac, R1 =Me, R2 =H). The latter is a useful tool in the solid-phase synthesis of the N-terminal sequence 3 of the leukemia-associated leukosialin.

ChemInform Abstract: Studies on the Biosynthesis of Paraherquamide. Construction of the Amino Acid Framework.

2010

Abstract It has been previously established in this laboratory that the β-methyl-β-hydroxyproline moiety of the potent anthelmintic agent paraherquamide A, is biosynthetically derived from l -isoleucine. The downstream events from l -Ile to paraherquamide A have now been investigated. The synthesis of [1- 13 C]-labeled l -β-methylproline is described by means of a Hoffman–Loeffler–Freytag reaction sequence from [1- 13 C]- l -Ile. This amino acid is shown to be a direct biosynthetic precursor to paraherquamide A by feeding and incorporation experiments in growing cultures of Penicillium fellutanum . Three tryptophan-containing dipeptides of l -β-methylproline have been constructed: [ 13 C 2 …

Polypeptide sequence of the chlorophyll a/b/c-binding protein of the prasinophycean alga Mantoniella squamata.

1994

The primary structure of the Chla/b/c-binding protein from Mantoniella squamata is determined. This is the first report that protein sequencing reveals one modified amino acid resulting in a LHCP-specific TFA-cleavage site. The comparison of the sequence of Mantoniella with other Chla/b-and Chla/c-binding proteins shows that the modified amino acid is located in a region which is highly conserved in all these proteins. The alignment also reveals that the LHCP of Mantoniella is related to the Chla/b-binding proteins. Finally, possible Chl-binding regions are discussed.

Chloroplastic glutamine synthetase from Brassica napus.

1993

Retention behaviour of paracelsin peptides on reversed-phase silicas with varying n-alkyl chain length and ligand density.

1989

As part of further investigations on the characterization of the ligand-induced conformational stabilization of peptides, two series of n-alkyldimethylsilyl bonded silicas have been prepared. In series A the n-alkyl chain length, n, of the bonded phase was varied between 1 and 20 carbon atoms at a constant ligand density. In series B the ligand density, alpha exp, was gradually changed from 0 to 4.1 mumol/m2 on a C1, C4, C6, C8 and C18 bonded phase. The retention behaviour of four peptides of the paracelsin family were examined under isocratic conditions, using a ternary mobile phase of water-methanol-acetonitrile (22:39:39, v/v/v). Plots of k' versus n showed pronounced maxima between n = …

Stabilization of an ?-helical conformation in an isolated hexapeptide inhibitor of calmodulin

2001

The conformational properties of two hexapeptides, Ac-LWRILW-NH(2) and its D-amino acid counterpart Ac-lwrilw-NH(2), identified as calmodulin inhibitors using mixture-based synthetic combinatorial library approaches, have been characterised by NMR and CD spectroscopy. The peptides fold into an alpha-helical conformation in aqueous solution. The observed short- and medium-range nuclear Overhauser effects were consistent with the formation of an alpha-helical structure and a reasonably well-defined set of structures was obtained by using restraints from the NMR data in simulated annealing calculations. Analysis of glycine-substitution analogues demonstrated that all the amino acids that make …

Influence of the hydrophilic face on the folding ability and stability of α-helix bundles: relevance to the peptide catalytic activity

2000

Although not the sole feature responsible, the packing of amino acid side chains in the interior of proteins is known to contribute to protein conformational specificity. While a number of amphipathic peptide sequences with optimized hydrophobic domains has been designed to fold into a desired aggregation state, the contribution of the amino acids located on the hydrophilic side of such peptides to the final packing has not been investigated thoroughly. A set of self-aggregating 18-mer peptides designed previously to adopt a high level of alpha-helical conformation in benign buffer is used here to evaluate the effect of the nature of the amino acids located on the hydrophilic face on the pa…

Sequence-specific and DNA structure-dependent interactions of Escherichia coli MutS and human p53 with DNA

2013

Many proteins involved in DNA repair systems interact with DNA that has structure altered from the typical B-form helix. Using magnetic beads to immobilize DNAs containing various types of structures, we evaluated the in vitro binding activities of two well-characterized DNA repair proteins, Escherichia coli MutS and human p53. E. coli MutS bound to double-stranded DNAs, with higher affinity for a G/T mismatch compared to a G/A mismatch and highest affinity for larger non-B-DNA structures. E. coli MutS bound best to DNA between pH 6 and 9. Experiments discriminated between modes of p53-DNA binding, and increasing ionic strength reduced p53 binding to nonspecific double-stranded DNA, but had…

Peptide metal-organic frameworks under pressure: flexible linkers for cooperative compression

2018

We investigate the structural response of a dense peptide metal-organic framework using in situ powder and single-crystal X-ray diffraction under high-pressures. Crystals of Zn(GlyTyr)2 show a reversible compression by 13% in volume at 4 GPa that is facilitated by the ability of the peptidic linker to act as a flexible string for a cooperative response of the structure to strain. This structural transformation is controlled by changes to the conformation of the peptide, which enables a bond rearrangement in the coordination sphere of the metal and changes to the strength and directionality of the supramolecular interactions specific to the side chain groups in the dipeptide sequence. Compar…