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Literature DB >> 24510645

Pulsed EPR distance measurements in soluble proteins by site-directed spin labeling (SDSL).

Ian Mitchelle S de Vera¹, Mandy E Blackburn^1,2, Luis Galiano^1,3, Gail E Fanucci¹.

Abstract

The resurgence of pulsed electron paramagnetic resonance (EPR) in structural biology centers on recent improvements in distance measurements using the double electron-electron resonance (DEER) technique. This unit focuses on EPR-based distance measurements by site-directed spin labeling (SDSL) of engineered cysteine residues in soluble proteins, with HIV-1 protease used as a model. To elucidate conformational changes in proteins, experimental protocols were optimized and existing data analysis programs were employed to derive distance-distribution profiles. Experimental considerations, sample preparation, and error analysis for artifact suppression are also outlined herein.

Entities: Chemical Disease Gene Species

Keywords: DEER; distance measurements; pulsed EPR; site-directed spin labeling

Mesh：

Substances：
Proteins
Spin Labels

Year: 2013 PMID： 24510645 PMCID： PMC4361181 DOI： 10.1002/0471140864.ps1717s74

Source DB: PubMed Journal: Curr Protoc Protein Sci ISSN： 1934-3655

79 in total

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3. The determination of pair distance distributions by pulsed ESR using Tikhonov regularization.

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8. Correlating conformational shift induction with altered inhibitor potency in a multidrug resistant HIV-1 protease variant.

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5. Genetic Incorporation of the Unnatural Amino Acid p-Acetyl Phenylalanine into Proteins for Site-Directed Spin Labeling.

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6. Mapping protein conformational heterogeneity under pressure with site-directed spin labeling and double electron-electron resonance.

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