19F Nuclear Magnetic Resonance Chemical Shifts of Fluorine Containing Aliphatic Amino Acids in Proteins: Studies on Lactobacillus casei Dihydrofolate Reductase Containing (2S,4S)-5-Fluoroleucine-Reference-Cited by-同舟云学术

19F Nuclear Magnetic Resonance Chemical Shifts of Fluorine Containing Aliphatic Amino Acids in Proteins: Studies on Lactobacillus casei Dihydrofolate Reductase Containing (2S,4S)-5-Fluoroleucine

Published:1996-01-01 Issue:36 Volume:118 Page:8700-8706
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Feeney James¹,McCormick John E.¹,Bauer Christopher J.¹,Birdsall Berry¹,Moody Claire M.¹,Starkmann Bernard A.¹,Young Douglas W.¹,Francis Peter¹,Havlin Robert H.¹,Arnold William D.¹,Oldfield Eric¹

Affiliation:

1. Contribution from the Molecular Structure Division and Biomedical NMR Centre, National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK, School of Chemistry and Molecular Sciences, University of Sussex, Falmer, Brighton, BN1 9QJ, UK, The Wellcome Research Laboratories, Langley Court, South Eden Park Road, Beckenham, Kent, BR3 3BS, UK, and Department of Chemistry, University of Illinois at Urbana-Champaign, 505 South Mathews Avenue, Urbana, Illinois 61801

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja960465i

Reference39 articles.

1. 4-Fluorotryptophan alkaline phosphatase from E.coli: Preparation, properties, and 19F NMR spectrum

2. Preparation and Studies of 19F-Labeled and Enriched 13C-Labeled Semisynthetic Ribonuclease-s' Analogues

3. Nuclear magnetic resonance and fluorescence studies of substrate-induced conformational changes of histidine-binding protein J of Salmonella typhimurium

4. [2] Deuteration in protein proton magnetic resonance

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