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

Ivan Peran; Matthew D. Watson; Osman Bilsel; Daniel P. Raleigh

doi:10.1039/c5cc08232c

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

Ivan Peran
, Matthew D. Watson
, Osman Bilsel
, Daniel P. Raleigh

Chemistry

Stony Brook University
University of Massachusetts Medical School

Research output: Contribution to journal › Article › peer-review

10 Scopus citations

Abstract

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

Original language	English
Pages (from-to)	2055-2058
Number of pages	4
Journal	Chemical Communications
Volume	52
Issue number	10
DOIs	https://doi.org/10.1039/c5cc08232c
State	Published - 2016

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10.1039/c5cc08232c

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title = "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.",

author = "Ivan Peran and Watson, \{Matthew D.\} and Osman Bilsel and Raleigh, \{Daniel P.\}",

note = "Publisher Copyright: {\textcopyright} The Royal Society of Chemistry 2016.",

year = "2016",

doi = "10.1039/c5cc08232c",

language = "English",

volume = "52",

pages = "2055--2058",

journal = "Chemical Communications",

issn = "1359-7345",

number = "10",

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TY - JOUR

T1 - Selenomethionine, p-cyanophenylalanine pairs provide a convenient, sensitive, non-perturbing fluorescent probe of local helical structure

AU - Peran, Ivan

AU - Watson, Matthew D.

AU - Bilsel, Osman

AU - Raleigh, Daniel P.

N1 - Publisher Copyright: © The Royal Society of Chemistry 2016.

PY - 2016

Y1 - 2016

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/84961299379

U2 - 10.1039/c5cc08232c

DO - 10.1039/c5cc08232c

M3 - Article

C2 - 26686928

AN - SCOPUS:84961299379

SN - 1359-7345

VL - 52

SP - 2055

EP - 2058

JO - Chemical Communications

JF - Chemical Communications

IS - 10

ER -

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

Abstract

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