Solution conformations of proline rings in proteins studied by NMR spectroscopy |
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Authors: | Mengli Cai Ying Huang Jianhua Liu Ramaswamy Krishnamoorthi |
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Institution: | (1) Department of Biochemistry, Kansas State University, 66506 Manhattan, KS, U.S.A. |
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Abstract: | Summary Three different conformations of proline rings in a protein in solution, Up, Down and Twist, have been distinguished, and stereospecific assignments of the pyrrolidine -, - and -hydrogens have been made on the basis of 1H-1H vicinal coupling constant patterns and intraresidue NOEs. For all three conformations, interhydrogen distances in the pairs -3, 3-3, 2-2, 2-2, and 3-3 (2.3 Å) are shorter than those in the pairs -2, 2-3, 3-2, 2-3, and 3-2 (2.7–3.0 Å), resulting in stronger NOESY cross peaks. For the Up conformation, the 3-2 and 2-3 spin-spin coupling constants are small (<3 Hz), and weak cross peaks are obtained in a short-mixing-time (10 ms) TOCSY spectrum; all other vicinal coupling constants are in the range 5–12 Hz, and result in medium to strong TOCSY cross peaks. For the Down form, the -2, 2-3, and 3-2 vicinal coupling constants are small, leading to weak TOCSY cross peaks; all other couplings again are in the range 5–12 Hz, and result in medium to strong TOCSY cross peaks. In the case of a Twist conformation, dynamically averaged coupling constants are anticipated. The procedure has been applied to bovine pancreatic trypsin inhibitor and Cucurbita maxima trypsin inhibitor-V, and ring conformations of all prolines in the two proteins have been determined. |
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Keywords: | Proline Conformation Protein Solution structure |
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