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A signal processing method to explore similarity in protein flexibility.


ABSTRACT: Understanding mechanisms of protein flexibility is of great importance to structural biology. The ability to detect similarities between proteins and their patterns is vital in discovering new information about unknown protein functions. A Distance Constraint Model (DCM) provides a means to generate a variety of flexibility measures based on a given protein structure. Although information about mechanical properties of flexibility is critical for understanding protein function for a given protein, the question of whether certain characteristics are shared across homologous proteins is difficult to assess. For a proper assessment, a quantified measure of similarity is necessary. This paper begins to explore image processing techniques to quantify similarities in signals and images that characterize protein flexibility. The dataset considered here consists of three different families of proteins, with three proteins in each family. The similarities and differences found within flexibility measures across homologous proteins do not align with sequence-based evolutionary methods.

SUBMITTER: Vasilache S 

PROVIDER: S-EPMC3010618 | biostudies-literature | 2010

REPOSITORIES: biostudies-literature

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A signal processing method to explore similarity in protein flexibility.

Vasilache Simina S   Mirshahi Nazanin N   Ji Soo-Yeon SY   Mottonen James J   Jacobs Donald J DJ   Najarian Kayvan K  

Advances in bioinformatics 20101220


Understanding mechanisms of protein flexibility is of great importance to structural biology. The ability to detect similarities between proteins and their patterns is vital in discovering new information about unknown protein functions. A Distance Constraint Model (DCM) provides a means to generate a variety of flexibility measures based on a given protein structure. Although information about mechanical properties of flexibility is critical for understanding protein function for a given protei  ...[more]

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