Conformational Studies on Modified Proteins and Peptides
نویسندگان
چکیده
منابع مشابه
Conformational Studies on Modified Proteins and Peptides IV. CONFORMATION OF LYSOZYME DERIVATIVES MODIFIED AT TYROSINE OR AT TRYPTOPHAN
Conformational investigations have been carried out on derivatives of lysozyme in which tyrosines 20 and 23 were nitrated (NTa-lysozyme), or in which the nitrotyrosine residues had been reduced to aminotyrosine (ATn-lysozyme). Also, a derivative modified at the 6 tryptophan residues by reaction with 2-nitrophenyl sulfenyl chloride (NPSe-lysozyme) was studied. In optical rotatory dispersion meas...
متن کاملConformational studies on modified proteins and peptides. IV. Conformation of lysozyme derivatives modified at tyrosine or at tryptophan residues.
Conformational investigations have been carried out on derivatives of lysozyme in which tyrosines 20 and 23 were nitrated (NTa-lysozyme), or in which the nitrotyrosine residues had been reduced to aminotyrosine (ATn-lysozyme). Also, a derivative modified at the 6 tryptophan residues by reaction with 2-nitrophenyl sulfenyl chloride (NPSe-lysozyme) was studied. In optical rotatory dispersion meas...
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Background and objectives: Tyrosinase is a copper containing oxidase which is crucial for controlling the production of melanin in creatures such as bacteria, fungi, plants and mammals. It is involved in the first two steps of melanin biosynthesis and leads to pigmentation and different types of cancer such as melanoma. Also, it is responsible for browning of fruits and vegetab...
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Conformational aspects of N-glycosylation of glycoproteins have been studied by using a series of peptides which contained, in addition to the ;marker sequence' Asn-Gly-Thr, two cysteine residues in various positions of the peptide chain. The presence of two cysteines permitted a partial fixation of the above triplet sequence in cyclic structures of various size by intramolecular disulphide bon...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1971
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)62226-4