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Hydrophobic amino acids in protein sequence
Hydrophobic amino acids in protein sequence





hydrophobic amino acids in protein sequence

Among them, six representative ones were successfully synthesized as peptides with reasonably high yields in a conventional Fmoc method, excluding the possibility that a putative physicochemical energy barrier in forming them could be a direct cause for the low availability.

hydrophobic amino acids in protein sequence hydrophobic amino acids in protein sequence

Nonexistent short sequences of pentats were found that showed low availability in biological proteins against their expected probabilities of occurrence. In a systematic attempt to reveal protein-database characters that could contribute to revealing how protein chains are constructed, frequency distributions of all possible combinatorial sets of three, four, and five amino acids (“triplets,” “quartets,” and “pentats” collectively called constituent sequences) have been examined in the nonredundant (nr) protein database, demonstrating the existence of nonrandom bias in their “availability” at the population level. Although used extensively for similarity searches, protein databases themselves have not fully been characterized. Much attention is being paid to protein databases as an important information source for proteome research.







Hydrophobic amino acids in protein sequence