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Literature DB >> 17067814

A quadrupole/time-of-flight mass spectrometry study of Trp-cage's conformation.

Mingxiang Lin¹, Zeeshan Ahmed, Christopher R Taormina, Kasi V Somayajula.

Abstract

Trp-cage is a synthetic 20-residue miniprotein that uses tertiary contacts to stabilize its native conformation. NMR, circular dichroism (CD), and UV-resonance Raman spectroscopy were used to probe its energy landscape. In this quadrupole/time-of-flight study, electrospray ionization charge state distribution (CSD) and solution-phase H/D exchange are used to probe Trp-cage's tertiary structure. The CSDs of Trp-cage and its mutant provide spectra showing a pH-dependent conformation change. Solution-phase H/D exchange in 30% deuterated trifluoroethanol solution of the wild type shows increased protection of one labile hydrogen in the native state. Together, CSDs and solution-phase H/D exchange are demonstrated to constitute a simple but effective means to follow conformation changes in a small tertiary protein.

Entities: Chemical

Mesh：

Substances：
Peptides
Trp-cage peptide

Year: 2006 PMID： 17067814 DOI： 10.1016/j.jasms.2006.09.001

Source DB: PubMed Journal: J Am Soc Mass Spectrom ISSN： 1044-0305 Impact factor: 3.109

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References

15 in total

1. Designing a 20-residue protein.

Authors: Jonathan W Neidigh; R Matthew Fesinmeyer; Niels H Andersen
Journal: Nat Struct Biol Date: 2002-06

2. The Trp cage: folding kinetics and unfolded state topology via molecular dynamics simulations.

Authors: Christopher D Snow; Bojan Zagrovic; Vijay S Pande
Journal: J Am Chem Soc Date: 2002-12-11 Impact factor: 15.419

3. Origin of the conformation dependence of protein charge-state distributions in electrospray ionization mass spectrometry.

Authors: Rita Grandori
Journal: J Mass Spectrom Date: 2003-01 Impact factor: 1.982

10. Charge state distribution and hydrogen/deuterium exchange of alpha-lactalbumin and beta-lactoglobulin preparations by electrospray ionization mass spectrometry.

Authors: Husam Alomirah; Inteaz Alli; Yasuo Konishi
Journal: J Agric Food Chem Date: 2003-03-26 Impact factor: 5.279

A quadrupole/time-of-flight mass spectrometry study of Trp-cage's conformation.

1. Designing a 20-residue protein.

2. The Trp cage: folding kinetics and unfolded state topology via molecular dynamics simulations.

3. Origin of the conformation dependence of protein charge-state distributions in electrospray ionization mass spectrometry.

4. Understanding folding and design: replica-exchange simulations of "Trp-cage" miniproteins.

Review 5. Studies of biomolecular conformations and conformational dynamics by mass spectrometry.

6. All-atom structure prediction and folding simulations of a stable protein.

7. Trp-cage: folding free energy landscape in explicit water.

8. Electron capture dissociation distinguishes a single D-amino acid in a protein and probes the tertiary structure.

9. UV-resonance raman thermal unfolding study of Trp-cage shows that it is not a simple two-state miniprotein.

10. Charge state distribution and hydrogen/deuterium exchange of alpha-lactalbumin and beta-lactoglobulin preparations by electrospray ionization mass spectrometry.