Results 11 to 20 of about 1,607,008 (329)
THE AMINO ACID SEQUENCE OF HYPERTENSIN II [PDF]
The Journal of Experimental Medicine, 1956 The amino acid sequence of horse hypertensin II has been determined by the use of chymotrypsin, the fluorodinitrobenzene method, and stepwise phenylisothiocyanate degradation. The results indicate that the amino acids of hypertensin II are arranged in the following order: asp-arg-val-tyr-iso-hist-pro-phe.
Leonard T. Skeggs +4 more
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The Amino Acid Sequence of Ribonuclease T1 [PDF]
Journal of Biological Chemistry, 1965 into other products. Glucoand galactocerebrosides, and ceramide trisaccharide, showed no activity (i.e. less than 300 cpm soluble in chloroform-methanol). Chloroform-methanolsoluble products were obtained with the following lipids: 4900 cpm with hematoside at 0.1 pmole per incubation mixture, and 7900 at 0.2 pmole; ceramide disaccharide, 720 cpm at 0.1
Kenji Takahashi
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Amino acid sequence of bacteriorhodopsin. [PDF]
Proceedings of the National Academy of Sciences, 1979 The complete primary structure of the purple membrane protein bacteriorhodopsin, which contains 248 amino acid residues, has been determined. Methods used for separation of the hydrophobic fragments included gel permeation and reverse-phase high-pressure liquid chromatography in organic solvents.
H G Khorana +6 more
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The amino acid sequence of human glucagon [PDF]
FEBS Letters, 1972 The amino acid sequence of bovine glucagon has been found to be the same as that reported for porcine glucagon [ 1,2] . Human glucagon has been isolated and crystallized [3] . The crystal form and the amino acid composition of human glucagon proved to be identical with those of porcine and bovine glucagon.
Johannes Thomsen +3 more
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The amino acid sequence of peanut agglutinin [PDF]
European Journal of Biochemistry, 1991 The amino acid sequence of peanut (Arachis hypogaea) agglutinin was determined from three major fragments obtained by mild acid cleavage at Asp‐Pro peptide bonds. The sequence of 236 amino acids has residues identical to those that form the metal‐binding site and the hydrophobic pocket in concanavlin A and other lectins, although the overall similarity
Young, N., Johnston, R., Watson, David
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Can Power Laws Help Us Understand Gene and Proteome Information?
Advances in Mathematical Physics, 2013 Proteins are biochemical entities consisting of one or more blocks typically folded in a 3D pattern. Each block (a polypeptide) is a single linear sequence of amino acids that are biochemically bonded together.
J. A. Tenreiro Machado +2 more
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STAR: predicting recombination sites from amino acid sequence
BMC Bioinformatics, 2006 Background Designing novel proteins with site-directed recombination has enormous prospects. By locating effective recombination sites for swapping sequence parts, the probability that hybrid sequences have the desired properties is increased ...
Thier Ricarda +3 more
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The signature motif of the Saccharomyces cerevisiae Pif1 DNA helicase is essential in vivo for mitochondrial and nuclear functions and in vitro for ATPase activity [PDF]
, 2018 Pif1 family DNA helicases are conserved from bacteria to humans and have critical and diverse functions in vivo that promote genome integrity. Pif1 family helicases share a 23 amino acid region, called the Pif1 signature motif (SM) that is unique to this
Galletto, Roberto +3 more
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Discovery of a Novel Member of the Carlavirus Genus from Soybean (Glycine max L. Merr.)
Pathogens, 2021 A novel member of the Carlavirus genus, provisionally named soybean carlavirus 1 (SCV1), was discovered by RNA-seq analysis of randomly collected soybean leaves in Illinois, USA.
Thanuja Thekke-Veetil +6 more
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Three classes of tetrahydrobiopterin-dependent enzymes
Pteridines, 2013 Current knowledge distinguishes three classes of tetrahydrobiopterin-dependent enzymes as based on protein sequence similarity. These three protein sequence clusters hydroxylate three types of substrate atoms and use three different forms of iron for ...
Werner Ernst R.
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