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Using 5-Hydroxytryptophan as a Probe to Follow Protein-Protein Interactions and Protein Folding Transitions

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5-Hydroxytyptophan is a fluorescent tryptophan analog that can be incorporated into recombinant proteins expressed in E. coli and is particularly useful in studies of biological systems that involve supermolecular aggregates of more than one protein. Here we review the varied applications of 5-hydroxytryptophan to study structure, interactions, conformational change and dynamics in complex protein systems.

Keywords: 5-hydroxytryptophan; fluorescence; protein folding; protein structure; protein-protein interactions; tryptophan

Document Type: Review Article


Affiliations: Departamento de Bioquimica, Instituto de Quimica, Universidade de Sao Paulo, Av. Prof. Lineu Prestes 748 Sao Paulo, SP, 05508-000, Brazil.

Publication date: April 1, 2005

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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