Journal article icon

Journal article

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

Abstract:

Experimental (15)N-(1)H and (1)H-(1)H residual dipolar couplings (RDCs) for the asparagine (Asn) and glutamine (Gln) side chains of hen egg-white lysozyme are measured and analysed in conjunction with (1)N relaxation data, information about chi(1) torsion angles in solution and molecular dynamics simulations. The RDCs are compared to values predicted from 16 high-resolution crystal structures. Two distinct groups of Asn and Gln side chains are identified. The first contains residues whose sid...

Expand abstract
Publication status:
Published

Actions


Access Document


Publisher copy:
10.1007/s10858-004-3218-y

Authors


More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Inorganic Chemistry
Role:
Author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Role:
Author
Journal:
Journal of biomolecular NMR
Volume:
30
Issue:
3
Pages:
327-346
Publication date:
2004-11-05
DOI:
EISSN:
1573-5001
ISSN:
0925-2738
URN:
uuid:44c3c18e-629e-4379-a601-799138c644d3
Source identifiers:
33020
Local pid:
pubs:33020

Terms of use


Metrics


Views and Downloads






If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP