Unknown

Dataset Information

0

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


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.

SUBMITTER: Peran I 

PROVIDER: S-EPMC4755734 | biostudies-literature | 2016 Feb

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

Peran Ivan I   Watson Matthew D MD   Bilsel Osman O   Raleigh Daniel P DP  

Chemical communications (Cambridge, England) 20160201 10


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. ...[more]

Similar Datasets

| S-EPMC4195376 | biostudies-other
| S-EPMC4357573 | biostudies-literature
| S-EPMC6566363 | biostudies-literature
| S-EPMC5717618 | biostudies-literature
| S-EPMC5392752 | biostudies-literature
| S-EPMC11355485 | biostudies-literature
| S-EPMC10452146 | biostudies-literature
| S-EPMC5972818 | biostudies-literature
| S-EPMC4874256 | biostudies-literature
| S-EPMC2873857 | biostudies-literature