A Solid State 13C NMR, Crystallographic, and Quantum Chemical Investigation of Phenylalanine and Tyrosine Residues in Dipeptides and Proteins-Reference-Cited by-同舟云学术

A Solid State 13C NMR, Crystallographic, and Quantum Chemical Investigation of Phenylalanine and Tyrosine Residues in Dipeptides and Proteins

Published:2007-05-17 Issue:23 Volume:129 Page:7385-7392
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Mukkamala Dushyant¹,Zhang Yong¹,Oldfield Eric¹

Affiliation:

1. Contribution from the Center for Biophysics and Computational Biology, 607 South Mathews Avenue, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, and Department of Chemistry, University of Illinois at Urbana-Champaign, 600 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/ja071227y

Reference41 articles.

1. Secondary and Tertiary Structural Effects on Protein NMR Chemical Shifts: an ab Initio Approach

2. Tryptophan Chemical Shift in Peptides and Proteins: A Solid State Carbon-13 Nuclear Magnetic Resonance Spectroscopic and Quantum Chemical Investigation

3. Expression of doubly labeled Saccharomyces cerevisiae iso -1 ferricytochrome c and 1 H, 13 C and 15 N chemical shift assignments by multidimensional NMR

4. Assignment and Analysis of Fluorine Nuclear Magnetic Resonance Spectra of 4-Fluorotryptophan Myoglobins and Hemoglobins

5. Chemical shifts in proteins: a shielding trajectory analysis of the fluorine nuclear magnetic resonance spectrum of the Escherichia coli galactose binding protein using a multipole shielding polarizability-local reaction field-molecular dynamics approach

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