عنوان
پدید آورنده
موضوع
رده
کتابخانه
محل استقرار
TLpq303702309
انگلیسی
Structure and conformational dynamics of turkey ovomucoid third domain by nuclear magnetic resonance spectroscopy
[Thesis]
A. D. Robertson
J. L. Markley
The University of Wisconsin - Madison
1988
200
Ph.D.
The University of Wisconsin - Madison
1988
Two-dimensional proton NMR experiments have been used to sequentially assign resonances to all of the peptide backbone protons of turkey ovomucoid third domain (OMTKY3) except those of the N-terminal S-amino group whose signal was not resolved owing to exchange with the solvent. Assignments also have been made for more than 80% of the side-chain protons. Two-dimensional chemical shift correlated spectroscopy (COSY), relayed coherence transfer spectroscopy (RELAY), and two-dimensional homonuclear Hartmann-Hahn spectroscopy (HOHAHA) were used to identify the spin systems of almost half of the residues prior to sequential assignment. Assignments were based on two-dimensional nuclear Overhauser enhancements observed between adjacent residues. The secondary structure of OMTKY3 in solution was determined from additional assigned NOESY cross-peaks; it closely resembles the secondary structure determined by single-crystal X-ray diffraction of OMTKY3 in complex with Streptomyces griseus proteinase B (Fujinaga, M., Read, R. J., Sielecki, A., Ardelt, W., Laskowski, M., Jr., and James, M. N. G. (1982) Proc. Natl. Acad. Sci. U.S.A. 79, 4868-4872). Through studies of the pH dependence for amide proton chemical shifts, we have confirmed pK{\rm a}\sp\prime values, originally determined by G. Ortiz-Polo ((1985) M. S. Thesis, Purdue University), for Glu-19, Asp-27, and Glu-43. The relative stabilities of the &-sheet and S-helix in OMTKY3 have been probed through study of the pH dependence for the exchange of over a dozen slowly exchanging amide protons.
Biochemistry
Pure sciences
A. D. Robertson
J. L. Markley
مطالعه متن کتاب p
[Thesis]
276903
a
Y
