Results 321 to 330 of about 1,122,450 (358)

Database of biologically active peptide sequences

Nahrung/Food, 1999
Proteins are sources of many peptides with diverse biological activity. Such peptides are considered as valuable components of foods with desired and designed biological activity. Two strategies are currently recommended for research in the area of biological activity of food protein fragments.
Jerzy Dziuba, D. Nałecz, Piotr Minkiewicz, Anna Iwaniak   +3 more
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Rapid sequence analysis of small peptides

Analytical Biochemistry, 1970
Abstract Small amounts of peptide material can be analyzed by a modified sequential degradation plus dansylation procedure. The method requires about 5 nanomoles per step, and is primarily designed for application to peptides of up to five or six residues.
Jean F. Smith, William R. Gray
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Sequence generation in prebiological peptide synthesis

Archives of Biochemistry and Biophysics, 1967
Abstract In contradistinction to the suggestion that peptide synthesis occurring nonenzymically on the primitive Earth would be a totally random event, evidence is presented that the interaction of any one given amino acid with another follows well-defined statistics based on the relative reactivity of each amino acid. The effects of environment, pH,
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Microfluidic Superheating for Peptide Sequence Elucidation

Analytical Chemistry, 2015
Herein, we introduce microfluidic superheating as a new method for peptide fragmentation prior to mass spectrometric analysis. The superheating conditions were found to be stable up to 240 °C for more than 30 min without elevated pressure or boiling of the aqueous sample. As proof of principle, we exposed the peptides ACTH1-10 and OVA257-264 to various
Matthias Altmeyer, Matthias Altmeyer, Andreas Manz, Pavel Neužil, Pavel Neužil   +4 more
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Peptimmunology: Immunogenic Peptides and Sequence Redundancy

Current Drug Discovery Technologies, 2005
Using short peptide fragments of proteins to elicit antibodies able to recognize the protein from which the peptide sequence was derived, is one of the main goals in immunotherapy today. Indeed, peptide-immunotherapy appears as an obliged way to obtain antibodies of predetermined specificity and exempt from the complications associated with whole cells/
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Mass spectrometric peptide sequencing: Cyclochlorotine

Biological Mass Spectrometry, 1979
A potent toxin isolated from Penicillium islandicum Sopp was found to have the composition C24H31N5O7Cl2. Mass spectrometric investigation of a partial acid hydrolyzate showed that it has the structure of cyclochlorotine. The mass spectral characteristics of polyamino alcohol-related derivatives of peptides containing beta-phenylalanine, alpha-amino ...
Klaus Biemann, Robert J. Anderegg, Anil C. Ghosh, Awinash Manmade   +3 more
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Polypeptide Helices in Hybrid Peptide Sequences

Journal of the American Chemical Society, 2005
A new class of polypeptide helices in hybrid sequences containing alpha-, beta-, and gamma-residues is described. The molecular conformations in crystals determined for the synthetic peptides Boc-Leu-Phe-Val-Aib-betaPhe-Leu-Phe-Val-OMe 1 (betaPhe: (S)-beta3-homophenylalanine) and Boc-Aib-Gpn-Aib-Gpn-OMe 2(Gpn: 1-(aminomethyl)cyclohexaneacetic acid ...
Ananda, Kuppanna, Vasudev, Prema G, Sengupta, Anindita, Poopathi Raja, K Muruga, Shamala, Narayanaswamy, Balaram, Padmanabhan   +5 more
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[17] Sequence analysis of phosphotyrosine-containing peptides

1991
Publisher Summary This chapter discusses the sequence analysis of phosphotyrosine-containing peptides. Phosphorylation of distinct tyrosine residues is an essential step in the response on stimulation of cells with a variety of hormones and growth factors.
Meyer HE, Hoffmann Posorske E, DONELLA, ARIANNA, Korte H.   +3 more
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Inhibition of peptide amyloid formation by cationic peptides with homologous sequences

Bioorganic & Medicinal Chemistry Letters, 2003
We have studied the model peptides that undergo self-initiated structural transition from alpha-helix to beta-sheet and self-assembling into amyloid fibrils. We here constructed an inhibition system of amyloid formation utilizing homologous recognition and assembly of peptides with increased solubility.
T. Yamashita, Y. Takahashi, T. Takahashi, H. Mihara   +3 more
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Protein and Peptide Sequence Determination

1983
In 1950 Edman published a chemical method for the stepwise removal of amino acids from the N-terminus of a peptide.1 This series of reactions has come to be known as the Edman Degradation, and although modifications of this technique have been introduced from time to time, (see below) the Edman Degradation remains, thirty years after its introduction ...
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