結構變化在各種具有重要生物功能的蛋白質交互作用間廣泛的被觀察到，舉例來說：adenylate kinase (AdK)催化ATP分解成AMP及磷酸的轉移，過程中產生巨大的結構轉變 (從開放狀態轉換至封閉狀態)，此結構轉換可能與基質或配體結合與後轉錄調控有關，如：磷酸化。已有許多研究將蛋白質特性可視化，如：將蛋白質每個胺基酸之演化保留度以圖形顯示。但大部份的研究皆著眼於蛋白質本質特性，而非蛋白質結構轉變。
本研究提供精緻且人性化的使用者介面，使用者可使用互動式圖表與3D立體結構來觀察結構轉變，使用者可以看到蛋白質結合造成的結構轉變，同時，本研究也提供了全面性的資訊，包含：sequence domains、structural domains、phosphorylation sites、catalytic sites、secondary structures、disorder regions、conservation profile以及hydrophathy profile。使用者可以深入探討各種生物特性間的關聯，本篇研究也將有利於各領域的探討，如：protein disorder、secondary structure transition、protein flexibility/plasticity、protein interaction、post-translational modification與molecular dynamics。

Proteins play important roles in many biological processes. These biological processes are conducted by a series of protein interactions with various molecules like proteins, ions or ligands. Many proteins undergo conformational changes upon these interactions, where regions with large conformational changes are critical to the interactions. This work presents the CCProf platform, which provides conformational changes of entire proteins, named conformational change profile (CCP) in the context. CCProf aims to be a platform where users can study potential causes of novel conformational changes. It provides ten biological features, including conformational change, potential binding target site, secondary structure, conservation, disorder propensity, hydropathy propensity, sequence domain, structural domain, phosphorylation site and catalytic site. All these information are integrated into a unified and well aligned view so that researchers can capture important relevance between different biological features visually. CCProf contains 41568 structure pairs for 3638 proteins. In addition, CCProf provides a 3D view in which users can see the structures before and after conformational changes as well as binding targets that induce conformational changes. All information (e.g., CCP, binding targets and structures) shown in CCProf, including intermediate data are available for download to expedite further analyses.

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