期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 373, 期 1, 页码 211-218出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2007.07.061
关键词
protein conformational stability; beta-turn; proline; glycine
资金
- NIGMS NIH HHS [T32 GM 065088, R01 GM037039, T32 GM065088, R01 GM052483-09, GM 52483, R01 GM052483, R01 GM037039-20, R29 GM052483, GM 37039] Funding Source: Medline
Protein conformational stability is an important concern in many fields. Here, we describe a strategy for significantly increasing conformational stability by optimizing beta-turn sequence. Proline and glycine residues are statistically preferred at several beta-turn positions, presumably because their unique side-chains contribute favorably to conformational stability in certain P-turn positions. However, beta-turn sequences often deviate from preferred proline or preferred glycine. Therefore, our strategy involves replacing non-proline and non-glycine beta-turn residues with preferred proline or preferred glycine residues. Here, we develop guidelines for selecting appropriate mutations, and present results for five mutations (S31P, S42G, S48P, T76P, and Q77G) that significantly increase the conformational stability of RNase Sa. The increases in stability ranged from 0.7 kcal/mol to 1.3 kcal/mol. The strategy was successful in overlapping or isolated beta-turns, at buried (up to 50%) or completely exposed sites, and at relatively flexible or inflexible sites. Considering the significant number of U-turn residues in every globular protein and the frequent deviation of U-turn sequences from preferred proline and preferred glycine residues, this simple, efficient strategy will be useful for increasing the conformational stability of proteins. (C) 2007 Elsevier Ltd. All rights reserved.
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