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Volumn 47, Issue 2, 2008, Pages 324-326

Structure of the protein BPTI derived with NOESY in supercooled water: Validation and refinement of solution structures

Author keywords

Aromatic ring flipping; NMR spectroscopy; Protein structures; Structure elucidation; Supercooled water

Indexed keywords

CONFORMATIONS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; SOLUTIONS; X RAY CRYSTALLOGRAPHY;

EID: 38049061568     PISSN: 14337851     EISSN: None     Source Type: Journal    
DOI: 10.1002/anie.200702842     Document Type: Article
Times cited : (5)

References (26)
  • 13
    • 38049051603 scopus 로고    scopus 로고
    • [4b]
    • [4b]
  • 15
    • 38049090428 scopus 로고    scopus 로고
    • [4b]
    • [4b]
  • 18
    • 38049046892 scopus 로고    scopus 로고
    • The constraint input of Ref. [9a] was used using the same calculation protocol with and without low-temperature constraints.
    • b) The constraint input of Ref. [9a] was used using the same calculation protocol with and without low-temperature constraints.
  • 22
    • 38049005750 scopus 로고    scopus 로고
    • α, and C of residues 2 to 56 in three X-ray crystal structures (protein data bank entries 4PTI, 5PTI, and 6PTI) relative to their mean coordinates is 0.22 Å. The corresponding RMSD value calculated for backbone heavy atoms and molecular core side-chain heavy atoms is 0.23 Å.
    • α, and C of residues 2 to 56 in three X-ray crystal structures (protein data bank entries 4PTI, 5PTI, and 6PTI) relative to their mean coordinates is 0.22 Å. The corresponding RMSD value calculated for backbone heavy atoms and molecular core side-chain heavy atoms is 0.23 Å.
  • 23
    • 38049057011 scopus 로고    scopus 로고
    • See also information-theoretical analysis of distance constraints in the Supporting Information
    • See also information-theoretical analysis of distance constraints in the Supporting Information.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.