Detection of salt bridges to lysines in solution in barnase

Poul Erik Hansen; Michael P. Williamson; Andrea M. Hounslow; Joe Ford; Kyle Fowler; Max Hebditch

doi:10.1039/C3CC45602A

Detection of salt bridges to lysines in solution in barnase

Poul Erik Hansen, Michael P. Williamson, Andrea M. Hounslow, Joe Ford, Kyle Fowler, Max Hebditch

Kemi

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

Abstract

We show that salt bridges involving lysines can be detected by deuterium isotope effects on NMR chemical shifts of the sidechain amine. Lys27 in the ribonuclease barnase is salt bridged, and mutation of Arg69 to Lys retains a partially buried salt bridge. The salt bridges are functionally important.

Originalsprog	Engelsk
Tidsskrift	Chemical Communications
Vol/bind	49
Sider (fra-til)	9824-9826
Antal sider	3
ISSN	1359-7345
DOI	https://doi.org/10.1039/C3CC45602A
Status	Udgivet - 2013

Emneord

lysines
salt bridges
isotope effects
barnase
proteins

Link til dokument

10.1039/C3CC45602A

Citer dette

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title = "Detection of salt bridges to lysines in solution in barnase",

abstract = "We show that salt bridges involving lysines can be detected by deuterium isotope effects on NMR chemical shifts of the sidechain amine. Lys27 in the ribonuclease barnase is salt bridged, and mutation of Arg69 to Lys retains a partially buried salt bridge. The salt bridges are functionally important.",

keywords = "lysines, salt bridges, isotope effects, barnase, proteins, lysines, salt bridges, isotope effects, barnase, proteins",

author = "Hansen, {Poul Erik} and Williamson, {Michael P.} and Hounslow, {Andrea M.} and Joe Ford and Kyle Fowler and Max Hebditch",

year = "2013",

doi = "10.1039/C3CC45602A",

language = "English",

volume = "49",

pages = "9824--9826",

journal = "Chemical Communications",

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publisher = "Royal Society of Chemistry",

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T1 - Detection of salt bridges to lysines in solution in barnase

AU - Hansen, Poul Erik

AU - Williamson, Michael P.

AU - Hounslow, Andrea M.

AU - Ford, Joe

AU - Fowler, Kyle

AU - Hebditch, Max

PY - 2013

Y1 - 2013

N2 - We show that salt bridges involving lysines can be detected by deuterium isotope effects on NMR chemical shifts of the sidechain amine. Lys27 in the ribonuclease barnase is salt bridged, and mutation of Arg69 to Lys retains a partially buried salt bridge. The salt bridges are functionally important.

AB - We show that salt bridges involving lysines can be detected by deuterium isotope effects on NMR chemical shifts of the sidechain amine. Lys27 in the ribonuclease barnase is salt bridged, and mutation of Arg69 to Lys retains a partially buried salt bridge. The salt bridges are functionally important.

KW - lysines

KW - salt bridges

KW - isotope effects

KW - barnase

KW - proteins

KW - lysines

KW - salt bridges

KW - isotope effects

KW - barnase

KW - proteins

U2 - 10.1039/C3CC45602A

DO - 10.1039/C3CC45602A

M3 - Journal article

SN - 1359-7345

VL - 49

SP - 9824

EP - 9826

JO - Chemical Communications

JF - Chemical Communications

ER -