Melting proteins confined in nanodroplets with 10.6 μm light provides clues about early steps of denaturation-Reference-Cited by-同舟云学术

Melting proteins confined in nanodroplets with 10.6 μm light provides clues about early steps of denaturation

Published:2018 Issue:26 Volume:54 Page:3270-3273
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

El-Baba Tarick J.¹²³⁴,Fuller Daniel R.¹²³⁴,Woodall Daniel W.¹²³⁴,Raab Shannon A.¹²³⁴,Conant Christopher R.¹²³⁴,Dilger Jonathan M.⁵⁶⁷⁴^ORCID,Toker Yoni⁸⁹¹⁰¹¹,Williams Evan R.¹¹²¹³⁴^ORCID,Russell David H.¹¹⁴¹⁵⁴^ORCID,Clemmer David E.¹²³⁴^ORCID

Affiliation:

1. Department of Chemistry

2. Indiana University

3. 47401

4. USA

5. Spectrum Warfare Systems Department

6. NSWC Crane Division

7. Crane

8. Department of Physics and Inst. of Nanotechnology

9. Bar-Ilan University

10. Ramat-Gan 5290002

11. Israel

12. University of California

13. Berkeley

14. Texas A&M University

15. College Station

Abstract

Irradiation of protein molecules in nanodroplets with 10.6 μm laser light reveals details of conformer stabilities and unfolding pathways.

Funder

National Institutes of Health

Indiana University

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2018/CC/C7CC09829D

Reference48 articles.

1. Freeze-Dried Biomolecules: FT-ICR Studies of the Specific Solvation of Functional Groups and Clathrate Formation Observed by the Slow Evaporation of Water from Hydrated Peptides and Model Compounds in the Gas Phase

2. From Solution to the Gas Phase: Stepwise Dehydration and Kinetic Trapping of Substance P Reveals the Origin of Peptide Conformations

3. Conformation Changes of Proteins

4. Modifying enzyme activity and selectivity by immobilization

5. Inactivation of immobilized trypsin under dissimilar conditions produces trypsin molecules with different structures

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