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One‐ and two‐dimensional nmr spectral analysis of the consequences of single amino acid replacements in proteins
Author(s) -
Markley John L.,
Croll David H.,
Krishnamoorthi R.,
OrtizPolo Gilberto,
Westler William M.,
Bogard W. C.,
Laskowski M.
Publication year - 1986
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240300403
Subject(s) - nuclear magnetic resonance spectroscopy , amino acid residue , amino acid , chemistry , residue (chemistry) , peptide sequence , protein superfamily , pulse sequence , sequence (biology) , protein structure , biological system , nuclear magnetic resonance , biochemistry , stereochemistry , biology , physics , gene
The traditional approach of using homologous sequences to elucidate the role of specific amino acid residues in protein structure and function becomes more meaningful as the number of differences is minimized, with the limit being alteration of a single residue. For small proteins in solution, NMR spectroscopy offers a means of obtaining detailed information about each residue and its response to a given change in the protein sequence. Extraction of this information has been aided by recent progress in spectrometer technology (higher magnetic fields, more sensitive signal detection, more sophisticated computers) and experimental strategies (new NMR pulse sequences including multiple‐quantum and two‐dimensional NMR methods). The set of avian ovomucoid third domains, which consists of the third domain proper plus a short leader (connecting peptide) and has a maximum of 56 amino acid residues, offers an attractive system for developing experimental methods for investigating sequence‐structure and structure‐function relationships in proteins. Our NMR results provide examples of sequence effects on pK a ′ values, average conformation, and internal motion of amino acid side chains.