Normal carbon acid referencing for protein amide hydrogen exchange.

Normal carbon acid referencing for protein amide hydrogen exchange. Research Abstract Details 

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Normal carbon acid referencing for protein amide hydrogen exchange. Abstract Text:

David M LeMaster,Janet S Anderson,Griselda ,

Measurement of the exchange kinetics for amide hydrogens along the protein backbone continues to offer valuable insights into structural stability and conformational dynamics. Since such studies routinely compare samples that differ in solution conditions or mechanical handling, normalization of the relative exchange rates can present a potentially significant source of experimental uncertainty. The carbon acids 1,3-dimethylimidazolium cation and thiomethylacetonitrile exhibit base catalyzed exchange rates similar to those of the slowly exchanging amides, under conditions typical for protein studies. With 13C enrichment at the acidic carbon position to facilitate selective observation, such carbon acids offer practical internal calibration of exchange.

Normal carbon acid referencing for protein amide hydrogen exchange. Publishing Authors By Initials

DM LeMaster,JS Anderson,G ,

For similar thiazoles research abstracts see: thiazoles research

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Normal carbon acid referencing for protein amide hydrogen exchange. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Magnetic resonance in chemistry : MRC

VOLUME: 45

Page Numbers: 601-4

Journal Abbreviation:

ISSN: 0749-1581

DAY: 3

MONTH: Jul

YEAR: 2007

Normal carbon acid referencing for protein amide hydrogen exchange. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 9882600

Normal carbon acid referencing for protein amide hydrogen exchange. Keywords Mesh Terms:

KEYWORDS: Thiazoles

MESH TERMS: standards

Chemical & Substance for Abstract: Normal carbon acid referencing for protein amide hydrogen exchange. Information

Substance Name: Thiazoles

Registry Number: 0

Grant and Affiliation Information for Normal carbon acid referencing for protein amide hydrogen exchange.

AFFILIATION: Wadsworth Center, New York State Department of Health and Department of Biomedical Sciences, School of Public Health, University at Albany - SUNY, Empire State Plaza, Albany, New York, 12201 USA.

Country: England

AGENCY: United States NIGMS

GRANT: GM 64736

ACRONYM: GM

MEDLINETA: Magn Reson Chem

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