Amphiphilic Proteins & Peptides

University Of California-Los Angeles, Los Angeles CA

Investigators

Abstract

Intellectual Merit: Structural and computational methods will be applied to understand why some proteins undergo transitions from their soluble, globular structures to form insoluble, elongated fibrils. In previous work, we have shown that an essential feature of fibril structure is that the protein contains a short self-complementary sequence of amino acids. We developed a computer algorithm that accurately identifies such segments, and we have validated the algorithm by experiments, which show that the identified segments do in fact form fibrils. Our goal now is to determine the universe of fibril-forming proteins, which we term the amylome. Broader Impacts: The wider implications of the work include the following: (1) Protein fibrils can form the basis of new materials. (2) A UCLA course in Structural Molecular Biology is linked to this research. In the laboratory section, students learn hands-on protein structure determination. Graduates of this course now teach and carry out research at some 30 universities, colleges, and research institutes. UCLA has perhaps the most diverse student body of any university, and our course reflects the demography of the campus. We plan to recruit students to this course, and through it, to the field of structural molecular biology, from a wide range of backgrounds, particularly those from underrepresented minority groups.