The aim of the study was to investigate patterns within and among α1 and α2 chains of Homo Sapiens type I collagen. The sequences of amino acids on alpha 1 and alpha 2 chains of type I collagen were taken from the National Center for Biotechnology Information. The CLC Proteine Workbench software was used in the investigation of amino acids patterns on type I collagen (within and among chains). Forty-seven patterns of 2 to 7 amino acids were identified on each chain. The patterns comprised the top-three frequent amino acids: glycine, proline and alanine on both chains. Seventeen out of forty-seven patterns (36%) were common on both chains. The patterns identified on the α2 chain comprise more amino acids compared with the patterns identified on α1 chain. The analysis among type I collagen chains identified patterns of 3 to up to 7 amino acids. Almost 13% of patterns identified on analysis among chains were seen on both chains. Future researcher will be necessary for studying the existence of the same patterns on type I collagen on different species as well as the usefulness of start and end position of the pattern in characterization of repetition and/or cyclicity of amino acids.


Type I collagen, Homo sapiens, Pattern analysis.