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Side-chains:
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Ab initio:
GeNMR
Cyana
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Refinement:
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Fragment-based:
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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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Molecular dynamics:
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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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Protein disorder:
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Protein solubility:
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Default An NMR method to probe molecular influences of substrate loading in NRPS carrier proteins.

An NMR method to probe molecular influences of substrate loading in NRPS carrier proteins.

Related Articles An NMR method to probe molecular influences of substrate loading in NRPS carrier proteins.

Biochemistry. 2015 Jan 26;

Authors: Goodrich AC, Frueh DP

Abstract
Carrier proteins (CPs) play a central role in nonribosomal peptide (NRP) synthesis by shuttling covalently attached substrates between active sites. Understanding how the covalent attachment of a substrate (loading) influences the molecular properties of CPs is key to determining the mechanism of NRP synthesis. However, structural studies have been impaired by substrate hydrolysis. Here, we used nuclear magnetic resonance spectroscopy to monitor substrate loading of a CP and to overcome hydrolysis. Our results reveal the spectroscopic signature of substrate loading and provide evidence of molecular communication between an NRPS carrier protein and its covalently attached substrate.


PMID: 25620398 [PubMed - as supplied by publisher]



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