Long-range interactions within a nonnative protein.

Journal article

Protein folding and unfolding are coupled to a range of biological phenomena, from the regulation of cellular activity to the onset of neurodegenerative diseases. Defining the nature of the conformations sampled in nonnative proteins is crucial for understanding the origins of such phenomena. We have used a combination of nuclear magnetic resonance (NMR) spectroscopy and site-directed mutagenesis to study unfolded states of the protein lysozyme. Extensive clusters of hydrophobic structure exi...

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Authors: Klein-Seetharaman, J; Oikawa, M; Grimshaw, S; Wirmer, J; Duchardt, E

• Publication status: Published
• Journal: Science (New York, N.Y.)
• Volume: 295
• Issue: 5560
• Pages: 1719-1722
• Publication date: 2002-03-01
• DOI: 10.1126/science.1067680
• EISSN: 1095-9203
• ISSN: 0036-8075
• Language: English
• Keywords: Protein Denaturation; Cysteine; Tryptophan; Kinetics; Muramidase; Protein Structure, Secondary; Hydrophobic and Hydrophilic Interactions; Protein Structure, Tertiary; Protein Conformation; Animals; Amino Acid Substitution; Nuclear Magnetic Resonance, Biomolecular; Protein Folding; Mutagenesis, Site-Directed; Point Mutation; Disulfides; Glycine; Chickens