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Literature DB >> 26686928

Selenomethionine, p-cyanophenylalanine pairs provide a convenient, sensitive, non-perturbing fluorescent probe of local helical structure.

Ivan Peran¹, Matthew D Watson¹, Osman Bilsel², Daniel P Raleigh³.

Abstract

The use of selenomethionine (MSe)-p-cyanophenylalanine (FCN) pairs to probe protein structure is demonstrated. MSe quenches FCN fluorescence via electron transfer. Both residues can be incorporated recombinantly or by peptide synthesis. Time-resolved and steady-state fluorescence measurements demonstrate that MSe-FCN pairs provide specific local probes of helical structure.

Entities: Chemical Disease Gene

Mesh：

Substances：

Year: 2016 PMID： 26686928 PMCID： PMC4755734 DOI： 10.1039/c5cc08232c

Source DB: PubMed Journal: Chem Commun (Camb) ISSN： 1359-7345 Impact factor: 6.222

30 in total

1. Dynamic NMR line-shape analysis demonstrates that the villin headpiece subdomain folds on the microsecond time scale.

Authors: Minghui Wang; Yuefeng Tang; Satoshi Sato; Liliya Vugmeyster; C James McKnight; Daniel P Raleigh
Journal: J Am Chem Soc Date: 2003-05-21 Impact factor: 15.419

2. Effect of modulating unfolded state structure on the folding kinetics of the villin headpiece subdomain.

Authors: Scott H Brewer; Dung M Vu; Yuefeng Tang; Ying Li; Stefan Franzen; Daniel P Raleigh; R Brian Dyer
Journal: Proc Natl Acad Sci U S A Date: 2005-11-03 Impact factor: 11.205

3. High-resolution x-ray crystal structures of the villin headpiece subdomain, an ultrafast folding protein.

Authors: Thang K Chiu; Jan Kubelka; Regine Herbst-Irmer; William A Eaton; James Hofrichter; David R Davies
Journal: Proc Natl Acad Sci U S A Date: 2005-05-13 Impact factor: 11.205

4. Sub-microsecond protein folding.

Authors: Jan Kubelka; Thang K Chiu; David R Davies; William A Eaton; James Hofrichter
Journal: J Mol Biol Date: 2006-03-31 Impact factor: 5.469

Review 5. Expanding the genetic code.

Authors: Lei Wang; Jianming Xie; Peter G Schultz
Journal: Annu Rev Biophys Biomol Struct Date: 2006

6. An unlocking/relocking barrier in conformational fluctuations of villin headpiece subdomain.

Authors: Andreas Reiner; Peter Henklein; Thomas Kiefhaber
Journal: Proc Natl Acad Sci U S A Date: 2010-03-01 Impact factor: 11.205

7. Making connections between ultrafast protein folding kinetics and molecular dynamics simulations.

Authors: Troy Cellmer; Marco Buscaglia; Eric R Henry; James Hofrichter; William A Eaton
Journal: Proc Natl Acad Sci U S A Date: 2011-03-24 Impact factor: 11.205

8. Modulation of p-cyanophenylalanine fluorescence by amino acid side chains and rational design of fluorescence probes of alpha-helix formation.

Authors: Humeyra Taskent-Sezgin; Peter Marek; Rosanne Thomas; Daniel Goldberg; Juah Chung; Isaac Carrico; Daniel P Raleigh
Journal: Biochemistry Date: 2010-07-27 Impact factor: 3.162

Selenomethionine, p-cyanophenylalanine pairs provide a convenient, sensitive, non-perturbing fluorescent probe of local helical structure.

1. Dynamic NMR line-shape analysis demonstrates that the villin headpiece subdomain folds on the microsecond time scale.

2. Effect of modulating unfolded state structure on the folding kinetics of the villin headpiece subdomain.

3. High-resolution x-ray crystal structures of the villin headpiece subdomain, an ultrafast folding protein.

4. Sub-microsecond protein folding.

Review 5. Expanding the genetic code.

6. An unlocking/relocking barrier in conformational fluctuations of villin headpiece subdomain.

7. Making connections between ultrafast protein folding kinetics and molecular dynamics simulations.

8. Modulation of p-cyanophenylalanine fluorescence by amino acid side chains and rational design of fluorescence probes of alpha-helix formation.

9. Photophysics of a Fluorescent Non-natural Amino Acid: p-Cyanophenylalanine.

10. Probing protein folding using site-specifically encoded unnatural amino acids as FRET donors with tryptophan.

Review 1. Meandering Down the Energy Landscape of Protein Folding: Are We There Yet?

2. Infrared and Fluorescence Assessment of Protein Dynamics: From Folding to Function.