DOI | Resolve DOI: https://doi.org/10.1007/978-94-011-1934-4_129 |
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Author | Search for: Fabian, Heinz; Search for: Naumann, Dieter; Search for: Schultz, Christian; Search for: Landt, Olfert; Search for: Hahn, Ulrich; Search for: Saenger, Wolfram; Search for: Mantsch, Henry H.1 |
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Affiliation | - National Research Council of Canada. NRC Institute for Biodiagnostics
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Format | Text, Book Chapter |
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Conference | The 5th European Conference on the Spectroscopy of Biological Molecules (ECSBM), September 5-10, 1993, Loutraki, Greece |
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Abstract | Ribonuclease T1 (RNase T1) is a small globular enzyme composed of 104 amino acids. Its three-dimensional structure is known and genetically-engineered overproducers are available (for a review see Ref. 1), which makes RNase T1 an excellent model system for investigating several aspects of protein folding. Various X-ray studies have shown that the secondary structure of RNase T1 includes a long α-helix, a major antiparallel β-sheet composed of three long and two short β-strands, a short two-stranded antiparallel β-sheet close to the N-terminus of the protein, and four wide loops which include several types of turns (Fig. 1). |
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Publication date | 1993 |
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In | |
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Language | English |
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NRC number | NRC-IBD-316 |
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NPARC number | 9742761 |
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Export citation | Export as RIS |
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Report a correction | Report a correction (opens in a new tab) |
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Record identifier | f84c3d03-f9d7-4f38-a3ce-db86bac5efc4 |
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Record created | 2009-07-17 |
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Record modified | 2020-06-10 |
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