Investigating the Secondary Structure of Membrane Peptides Utilizing Multiple 2H-Labeled Hydrophobic Amino Acids via Electron Spin Echo Envelope Modulation (ESEEM) Spectroscopy-Reference-Cited by-同舟云学术

Investigating the Secondary Structure of Membrane Peptides Utilizing Multiple 2H-Labeled Hydrophobic Amino Acids via Electron Spin Echo Envelope Modulation (ESEEM) Spectroscopy

Published:2018-04-03 Issue:16 Volume:122 Page:4388-4396
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Liu Lishan¹,Sahu Indra D.¹,Bottorf Lauren¹,McCarrick Robert M.¹,Lorigan Gary A.¹^ORCID

Affiliation:

1. Department of Chemistry and Biochemistry, Miami University, Oxford, Ohio 45056, United States

Funder

National Institute of General Medical Sciences

University of Miami

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.7b11890

Reference39 articles.

1. Probing the structure of membrane proteins with electron spin echo envelope modulation spectroscopy

2. Determining α-Helical and β-Sheet Secondary Structures via Pulsed Electron Spin Resonance Spectroscopy

3. Enhancement of Electron Spin Echo Envelope Modulation Spectroscopic Methods to Investigate the Secondary Structure of Membrane Proteins

4. Determining the Secondary Structure of Membrane Proteins and Peptides Via Electron Spin Echo Envelope Modulation (ESEEM) Spectroscopy

5. Development of electron spin echo envelope modulation spectroscopy to probe the secondary structure of recombinant membrane proteins in a lipid bilayer

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