ALBERT — All Library Books, journals and Electronic Records Telegrafenberg

Hits per page

hits 1 - 2 | 2 hits

Sorting

Electronic Resource

Evaluation of errors of interproton distances and correlation time determined from NMR cross-relaxation rates (1992)

Isernia, Carla ; Paolillo, Livio ; Russo, Ernesto ; [et al.]

Springer

Journal of biomolecular NMR 2 (1992), S. 573-582

add to mindlist on the mindlist

Details

ISSN: 1573-5001

Keywords: Amaninamide ; Correlation time ; Evaluation of errors ; Interproton distances ; NOESY ; ROESY ; 2D NMR ; Peptides ; Cross-relaxation

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Chemistry and Pharmacology

Notes: Summary We have analyzed a combined use of the two-dimensional nuclear Overhauser effect in the laboratory frame (NOESY) and in the rotating frame (ROESY) to determine interproton distances and correlation time in medium-sized rigid molecules (Davis, 1987). This method can be applied in the intermediate motional regime, 0.2 〈 ωoτc, 〈 5, (τc, correlation time, (ωo resonance frequency). Error limits depend on the motional regime and are smallest near ωoτc=1.14. The method was tested on six geminal proton pairs in the bicyclic octapeptide (S-deoxo-γ-[R]-OH-Ile3 amaninamide, Mw =870) for which at 297 K in DMSO, a correlation time of 1.0 ns, with a standard deviation of 0.12 ns, and an interproton distance of 1.87 Å, with standard deviation of 0.04 Å, are obtained.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF02192846

Permalink

	Location	Call Number	Expected	Availability

Others were also interested in ...

Paper (German National Licenses)

Fulltext

Electronic Resource

Conformational studies on synthetic peptides reproducing the dibasic processing site of pro-ocytocin-neurophysin (1995)

Di Bello, Carlo ; Simonetti, Mario ; Dettin, Monica ; [et al.]

New York, NY [u.a.] : Wiley-Blackwell

Journal of Peptide Science 1 (1995), S. 251-265

add to mindlist on the mindlist

Details

ISSN: 1075-2617

Keywords: Hormone biosynthesis ; ocytocin ; prohormone ; proteolytic processing ; β-turn ; Chemistry ; Biochemistry and Biotechnology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Chemistry and Pharmacology

Notes: Synthetic peptides reproducing the proteolytic processing site of pro-ocytocin were studied by different spectroscopic techniques, including circular dichroism, Fourier tranform infrared absorption, and mono and bidimensional nuclear magnetic resonance, in order to ascertain the possible role of three-dimensional structure in the recognition process by maturation enzymes. Experimental results were compared with energy minimization calculations and suggest that: (i) the region situated on the N-terminus of the Lys-Arg doublet may form a β-turn; (ii) the sequential organization of the residues participating in the β-turn determines the privileged relative orientation of the basic amino acid sidechains and the subtype of turn; and (iii) the peptide segment situated on the C-terminal side of the dibasic doublet may assume a helix arrangement. These findings, in spite of the limitations connected to the flexibility of linear peptides, seem to substantiate the hypothesis that structural motifs around the cleavage site could be important for recognition and processing. However, a straightforward correlation between details of the secondary structure and the in vitro reactivity toward a putative convertase is not yet possible.

Additional Material: 7 Ill.