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
Influence of glycine residues on peptide conformation in membran environments
β Scribed by LI, SHUN-CHENG ;DEBER, CHARLES M.
- Book ID
- 115099316
- Publisher
- Wiley (Blackwell Publishing)
- Year
- 2009
- Tongue
- English
- Weight
- 535 KB
- Volume
- 40
- Category
- Article
- ISSN
- 0367-8377
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π SIMILAR VOLUMES
Transmembrane segments (TM) are important structural elements that often define the functional domain of membrane proteins.'.2 Structural studies of TM segments are thus becoming essential for understanding the structure/ function of membrane proteins, although their physical properties have often c
## Abstract The mechanism of membrane interaction by Ξ²βsheet peptides is important to understand fundamental principles of folding of Ξ²βbarrel proteins and various Ξ²βamyloid proteins. Here, we examined the conformational characteristics of a porinβlike channel forming (__x__S__x__G)~6~ peptide in s