Iqbal, M. ; Balaram, P. (1982) The helical conformations of 14- and 16-residue fragments of suzukacillin, a membrane channel-forming polypeptide Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 706 (2). pp. 179-187. ISSN 0167-4838
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Official URL: http://linkinghub.elsevier.com/retrieve/pii/016748...
Related URL: http://dx.doi.org/10.1016/0167-4838(82)90485-X
Abstract
The suzukacillin fragments, Boc-Ala-Aib-Aib-Gln-Aib-Leu-Aib-Gly-Leu-Aib-Pro-Val-Aib-Aib-OMe (14), Boc-Ala-Aib-Ala-Aib-Aib-Gln-Aib-Leu-Aib-Gly-Leu-Aib-Pro-Val-Aib-Aib-OMe (16G) and the completely apolar 16-residue peptide in which the glutamine residue has been replaced by alanine (16A) have been studied by 270 MHz 1H-HMR, in C2HCl3 and (C2H3)2SO solution. Intramolecularly hydrogen-bonded NH groups have been identified by temperature and solvent dependence of chemical shifts. Peptides 14 and 16A adopt folded 310 helical conformations stabilized by 11 and 13 hydrogen bonds, respectively. In peptide 16G there are 12 intramolecular hydrogen bonds, with the glycine NH being solvent-exposed, in contrast to 14 and 16A.
| Item Type: | Article |
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| Source: | Copyright of this article belongs to Elsevier Science. |
| Keywords: | Suzukacillin Fragment; Helical Peptide; Oligopeptide Conformation; Membrane Channel; NMR |
| ID Code: | 5047 |
| Deposited On: | 18 Oct 2010 05:22 |
| Last Modified: | 16 May 2016 15:37 |
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