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Titolo:
H-1-NMR AND F-19-NMR APPROACHES TO THE STUDY OF THE STRUCTURE OF PROTEINS LARGER THAN 25-KDA
Autore:
GETTINS PGW;
Indirizzi:
UNIV ILLINOIS,DEPT BIOCHEM,M-C 536,1819-1853 W POLK ST CHICAGO IL 60612
Titolo Testata:
International journal of biological macromolecules
fascicolo: 5, volume: 16, anno: 1994,
pagine: 227 - 235
SICI:
0141-8130(1994)16:5<227:HAFATT>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEAR MAGNETIC-RESONANCE; HUMAN ANTITHROMBIN-III; A-ALPHA-CHAIN; FIBRINOGEN-LIKE PEPTIDES; ANTIBODY COMBINING SITE; EPIDERMAL GROWTH-FACTOR; D-LACTATE DEHYDROGENASE; HIGH-AFFINITY HEPARIN; SPIN-LABEL ANTIBODY; HORSERADISH-PEROXIDASE;
Keywords:
NUCLEAR MAGNETIC RESONANCE; PROTEINS; DIFFERENCE SPECTROSCOPY;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
73
Recensione:
Indirizzi per estratti:
Citazione:
P.G.W. Gettins, "H-1-NMR AND F-19-NMR APPROACHES TO THE STUDY OF THE STRUCTURE OF PROTEINS LARGER THAN 25-KDA", International journal of biological macromolecules, 16(5), 1994, pp. 227-235

Abstract

The three-dimensional solution structures of proteins larger than about 25 kDa cannot at present be detemined by multi-dimensional nuclear magnetic resonance (NMR) methods. However, for proteins that are larger than 25 kDa, for which X-ray structural information is not available, there are a variety of mostly one-dimensional NMR methods that stillrepresent some of the most informative approaches to obtaining structural answers to questions of biochemical interest. This paper providesrecent illustrative examples of H-1- and F-19-NMR experiments that describe ways to focus on proteins by region, by amino acid type, or by individual amino acid. Methods to focus on a particular region of a protein include exploiting domain mobility, using transferred nuclear Overhauser enhancements, the use of difference spectroscopy, the use of paramagnetic species, and domain fragmentation. Particular types of amino acid can be identified using selective deuteration, by incorporation of fluorinated amino acid analogues, by using photochemically induced dynamic nuclear polarization, and from the pH dependence of histidine residues. Individual amino acids can be identified by mutagenesis and, in special circumstances, by chemical shift. Many of the examples given are of plasma proteinases and their protein inhibitors, but other classes of protein are also discussed, including antibodies and DNA-binding proteins.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 22:41:17