Related Experiment Video
Updated: Jun 12, 2026

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
Published on: November 1, 2024
Frequencies of specific peptides in intrinsic disordered protein domains
Susan Costantini1, Maria Costantini, Giovanni Colonna
1Centro Ricerche Oncologiche di Mercogliano "Fiorentino Lo Vuolo", via Ammiraglio Bianco, 83013 Mercogliano (AV) Italy. susan.costantini@unina2.it
Abstract:
We evaluated the i-peptides occurrence frequency in the protein sequences, belonging to two reference datasets containing structured and disordered protein domains. Moreover we estimated the most frequent i-peptides (with i= 2, 3, 4) into these sequences in order to select specific i-peptides for each structural classification. According to these specific i-peptides, a new binary classification method was developed for predicting if a given protein sequence can be classified as "disordered" or "structured". The best results were obtained using the tri-peptides, much more able to gain structural information from sequences compared to the di-peptides.
More Related Videos
Related Concept Videos
Intrinsically Disordered Proteins
Intrinsically Disordered Proteins
Conservation of Protein Domains Over Different Proteins
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Conserved Binding Sites
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding

