Results 231 to 240 of about 257,506 (253)
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Motifs and conformational analysis of amino acid residues adjoining β‐turns in proteins

International Journal of Peptide and Protein Research, 1996
Using a data set of 250 non‐homologous high‐resolution globular proteins, a systematic analysis of the conformations that precede and succeed (positions i and i+3) the various classical β‐turn types has been carried out. The collective conformation of a specific β‐turn type, including the flanking positions, termed motif, has been studied.
Ramakrishnan, C   +2 more
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Discovery of Amino Acid Motifs for Thrombin Cleavage and Validation Using a Model Substrate

Biochemistry, 2011
Understanding the active site preferences of an enzyme is critical to the design of effective inhibitors and to gaining insights into its mechanisms of action on substrates. While the subsite specificity of thrombin is understood, it is not clear whether the enzyme prefers individual amino acids at each subsite in isolation or prefers to cleave ...
Natasha M, Ng   +9 more
openaire   +2 more sources

Aromatic Amino Acids Providing Characteristic Motifs in the Raman and SERS Spectroscopy of Peptides

The Journal of Physical Chemistry B, 2008
Raman and surface-enhanced Raman spectroscopies (SERS) are potentially important tools in the characterization of biomolecules such as proteins and DNA. In this work, SERS spectra of three cysteine-containing aromatic peptides: tryptophan-cysteine, tyrosine-cysteine, and phenylalanine-cysteine, bound to Au nanoshell substrates, were obtained, and ...
Fang, Wei   +3 more
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The Use of Extended Amino Acid Motifs for Focussing on Toxic Peptides in Coeliac Disease

The Journal of Biochemistry, Molecular Biology and Biophysics, 2002
Cereal prolamins of wheat, rye and barley are the major proteins that have been implicated in toxicity in patients with coeliac disease. The gliadins of wheat are the best characterised with the identification of toxic peptides from rye and barley not as well advanced. This study has employed extended motifs, based on the known toxic motifs are derived
A, McLachlan, P G, Cullis, H J, Cornell
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Unnatural amino acids in the synthesis and semisynthesis of metalloprotein motifs

1994
The design, synthesis, and characterization of two novel metalloprotein motifs is presented. The first project involved the design and construction of a protein motif which was programmed to form a tetradentate metal complex upon the addition of metal cations.
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Covariance analysis of RNA recognition motifs identifies functionally linked amino acids

Journal of Molecular Biology, 2001
The RNA recognition motif (RRM) is one of the most common eukaryotic protein motifs. RRM sequences form a conserved globular structure known as the RNA-binding domain (RBD) or the ribonucleoprotein domain. Many proteins that contain RRM sequences bind RNA in a sequence-specific manner.
S, Crowder, J, Holton, T, Alber
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The Functional Motifs That Are Revealed in the Gypsy Gag Amino Acid Sequence

Doklady Biochemistry and Biophysics, 2004
B V, Syomin, Y V, Ilyin
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Identification of protein motifs using conserved amino acid properties and partitioning techniques.

Proceedings. International Conference on Intelligent Systems for Molecular Biology, 1995
Analyzing a set of protein sequences involves a fundamental relationship between the coherency of the set and the specificity of the motif that describes it. Motifs may be obscured by training sets that contain incoherent sequences, in part due to protein subclasses, contamination, or errors.
Thomas D. Wu, Douglas L. Brutlag
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