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عنوان
Structure and conformational dynamics of turkey ovomucoid third domain by nuclear magnetic resonance spectroscopy

پدید آورنده
A. D. Robertson

موضوع
Biochemistry,Pure sciences

رده

کتابخانه
کتابخانه مطالعات اسلامی به زبان های اروپایی

محل استقرار
استان: قم ـ شهر: قم

کتابخانه مطالعات اسلامی به زبان های اروپایی

تماس با کتابخانه : 32910706-025

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

الاقتراح / اعلان الخلل

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