Abstract:
:The D/H fractionation factor (sigma) is the extent to which a hydrogen at a particular site becomes enriched in 2H over 1H relative to the solvent. A growing body of experimental evidence suggest that there is a correlation between the value of the fractionation factor and hydrogen-bond strength, with a lower sigma value reflecting a stronger hydrogen bond. Fractionation factors of 60% of the individual backbone amide hydrogens in the staphylococcal nuclease V8 variant (H124L) have been measured for the enzyme in the presence and absence of bound ligands (the activating ion Ca2+ and the inhibitor thymidine 3',5'-bisphosphate). The method used employed two-dimensional 1H-15N nuclear magnetic resonance analysis of uniformly 15N-labeled protein in mixed H2O/D2O solvents. Fractionation factors of individual residues were found to range from 0.3 (T120) to 1.5 (L38). The sigma value of 0.3 for the NH of T120, which is the lowest fractionation factor reported for any system yet studied, suggests that the hydrogen bond between T120 HN and D77 O delta 1 is unusually strong. The results of previous site-directed mutagenesis experiments [Hinck, A. P. (1993) Ph.D. Thesis, University of Wisconsin-Madison, Madison, WI] support the notion that formation of this hydrogen bond is important to maintain the stability and conformation of the native state. The sigma value averaged over all residues was approximately 0.85 for both the unligated and ligated enzymes. Residues in alpha-helices displayed a slightly lower average sigma value (0.79), whereas residues with solvent-exposed amide hydrogens exhibited a slightly higher average figure (0.98).(ABSTRACT TRUNCATED AT 250 WORDS)
journal_name
Biochemistryjournal_title
Biochemistryauthors
Loh SN,Markley JLdoi
10.1021/bi00170a023subject
Has Abstractpub_date
1994-02-01 00:00:00pages
1029-36issue
4eissn
0006-2960issn
1520-4995journal_volume
33pub_type
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