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Ab initio:
GeNMR
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Fragment-based:
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Refinement:
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Structure from chemical shifts:
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Torsion angles from chemical shifts:
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Secondary structure from chemical shifts:
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Flexibility from chemical shifts:
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From structure:
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From sequence:
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Disordered proteins:
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Format conversion & validation:
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From NMR-STAR 3.1
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NMR sample preparation:
Protein disorder:
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Protein solubility:
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Isotope labeling:
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Solid-state NMR:
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Old 08-22-2010, 02:20 PM
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Default Solution structure of regioselectively addressable functionalized templates: an NMR a

Solution structure of regioselectively addressable functionalized templates: an NMR and restrained molecular dynamics investigation.

Related Articles Solution structure of regioselectively addressable functionalized templates: an NMR and restrained molecular dynamics investigation.

Biopolymers. 1996 Sep;39(3):297-308

Authors: Dumy P, Eggleston IM, Esposito G, Nicula S, Mutter M

Three cyclic peptides that are Regioselectively Addressable Functionalized Templates (RAFT) for use in protein de novo design have been investigated using a combination of nmr, restrained molecular dynamics, and CD spectroscopy. These peptides contain up to four selectively addressable sites (orthogonally protected lysine side chains) or have selectively addressable faces. The results show a common stable conformation for templates of this kind based on two type II beta-turns and an associated beta-sheet structure. A preferential orientation for the side chains is also demonstrated. The significance of these findings is discussed in the context of applications of RAFT that rely on their conformational rigidity and ability to present functionalities in a defined spatial arrangement.

PMID: 8756511 [PubMed - indexed for MEDLINE]



Source: PubMed
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