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Research papers - Hydration, mobility and accessibility of lysozyme: Structures of a pH 6.5 orthorhombic form and its low-humidity variant and a comparative study involving 20 crystallographically independent molecules - X-ray analyses and a comparative study of a large number of crystal structures of lysozyme show that the changes in the molecular geometry and hydration of the enzyme caused by variation in the amount of surrounding water are more pronounced than those caused by change in pH. They also lead to information on the flexibility and accessibility of the molecule and the role of invariant water molecules including those at the catalytic site/
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| No. | 권호·제본정보 보기 | 소장처 | 소장사항 | 청구기호 | 구독 | 최근입수호 |
|---|---|---|---|---|---|---|
| 1 | 중앙도서관/3층 연속간행물(보존)/ | 548.05 A188D | ||||
| 2 | 중앙도서관/3층 연속간행물실/ | 548.05 A188D | 구독중단 | Vol.56 No.12 |
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