Asparagine and glutamine side-chain conformation in solution and crystal: A comparison for hen egg-white lysozyme using residual dipolar ouplings

Victoria Ann Higman; Jonathan Boyd; Lorna J. Smith; Christina Redfield

doi:10.1007/s10858-004-3218-y

Keywords

AsparagineChemistryLysozymeGlutamineSide chainResidual dipolar couplingDipoleResidualCrystallographyBiochemistryEnzymeAmino acidOrganic chemistryPolymer

Affiliated Institutions

University of Oxford GB

Related Publications

Insights into the Mobility of Methyl-Bearing Side Chains in Proteins from 3JCC and 3JCN Couplings

James J. Chou , David A. Case , Ad Bax

Side-chain dynamics in proteins can be characterized by the NMR measurement of (13)C and (2)H relaxation rates. Evaluation of the corresponding spectral densities limits the slo...

2003 Journal of the American Chemical Society 131 citations

Structure and Dynamics of the Homologous Series of Alanine Peptides: A Joint Molecular Dynamics/NMR Study

Jürgen Graf , Phuong H. Nguyen , Gerhard Stock +1 more

The phi,psi backbone angle distribution of small homopolymeric model peptides is investigated by a joint molecular dynamics (MD) simulation and heteronuclear NMR study. Combinin...

2007 Journal of the American Chemical Society 331 citations

The Examination of the Presence of Amide Groups in Glutamic Acid and Aspartic Acid Residues of Staphylococcal Nuclease (Foggi Strain)

Janice L. Bohnert , Hiroshi Taniuchi

Abstract The presence and absence of amide groups at 5 aspartic acid and 4 glutamic acid residues of the amino acid sequence of staphylococcal nuclease (Foggi strain) has been d...

1972 Journal of Biological Chemistry 22 citations

ff14SB: Improving the Accuracy of Protein Side Chain and Backbone Parameters from ff99SB

James Maier , Carmenza Martinez , Koushik Kasavajhala +3 more

Molecular mechanics is powerful for its speed in atomistic simulations, but an accurate force field is required. The Amber ff99SB force field improved protein secondary structur...

2015 Journal of Chemical Theory and Comput... 10209 citations

Location of the Heme in Horse Heart Ferricytochrome c by X-Ray Diffraction

Richard E. Dickerson , Mary L. Kopka , J. Weinzierl +3 more

Abstract A low resolution (4A) electron density map of horse heart cytochrome c crystals has been obtained by x-ray diffraction methods. The molecule is a prolate spheroid, appr...

1967 Journal of Biological Chemistry 143 citations

Publication Info

Year: 2004
Type: article
Volume: 30
Issue: 3
Pages: 327-346
Citations: 21
Access: Closed

External Links

View on DOI.org

Social Impact

Altmetric

Asparagine and glutamine side-chain conformation in solution and crystal: A comparison for hen egg-white lysozyme using residual dipolar ouplings

PlumX Metrics

Social media, news, blog, policy document mentions

Citation Metrics

OpenAlex

Cite This

APA Style

                            
                                
                                    Victoria Ann Higman, 
                                
                                    Jonathan Boyd, 
                                
                                    Lorna J. Smith
                                
                                et al.
                            
                            (2004). 
                            Asparagine and glutamine side-chain conformation in solution and crystal: A comparison for hen egg-white lysozyme using residual dipolar ouplings. 
                            Journal of Biomolecular NMR
                            , 30
                            (3)
                            , 327-346.
                            https://doi.org/10.1007/s10858-004-3218-y
                        

Identifiers

DOI: 10.1007/s10858-004-3218-y