Conformation of proline residues in bacteriorhodopsin
โ Scribed by Charles M. Deber; Barbara J. Sorrell; Guang-Yi Xu
- Book ID
- 115762921
- Publisher
- Elsevier Science
- Year
- 1990
- Tongue
- English
- Weight
- 524 KB
- Volume
- 172
- Category
- Article
- ISSN
- 0006-291X
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๐ SIMILAR VOLUMES
Although noted as hydrophilic residues with helix-breaking potential, proline residues are observed in putatively a-helical transmembrane (TM) segments of many channel-forming integral membrane proteins. In addition to the recognized property of X-Pro peptide bonds (where X = any amino acid) to occu
Semiempirical AM1 calculations were performed for quantum chemically ลฝ . optimized minimum-energy conformations of L-alanine oligomers A at n s 7 and n their derivatives containing one, two, or three proline residues at various positions along the peptide chain. The effect of proline residues on the