Abstract:
:Synthetic model membrane-interactive peptides--both of natural and designed sequence--have become convenient and systematic tools for determination of how the membrane-spanning segments within integral membrane proteins confer protein structure and biology. Conformational studies on these peptides demonstrate that the alpha-helix is the natural choice of conformation for a peptide segment in a membrane, and that a helical conformation will arise "automatically" in a peptide above a threshold hydrophobicity that allows it to associate stably with the membrane. Environmental and sequential contexts thus impart conformational versatility to many of the amino acids, thereby providing a mechanism for producing the diverse structural and functional properties of proteins.
journal_name
Biopolymersjournal_title
Biopolymersauthors
Deber CM,Li SCdoi
10.1002/bip.360370503subject
Has Abstractpub_date
1995-01-01 00:00:00pages
295-318issue
5eissn
0006-3525issn
1097-0282journal_volume
37pub_type
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