Journal article icon

Journal article

Conformational dynamics of helix S6 from Shaker potassium channel: simulation studies.

Abstract:

Prolines in transmembrane (TM) alpha-helices are believed to play an important structural and/or functional role in membrane proteins. At a structural level a proline residue distorts alpha-helical structure due to the loss of at least one stabilizing backbone hydrogen bond, and introduces flexibility in the helix that may result in substantial kink and swivel motions about the effective "hinge." At a functional level, for example in Kv channels, it is believed that proline-induced molecular ...

Expand abstract
Publication status:
Published

Actions


Access Document


Publisher copy:
10.1002/bip.10197

Authors


Journal:
Biopolymers
Volume:
64
Issue:
6
Pages:
303-313
Publication date:
2002-09-05
DOI:
EISSN:
1097-0282
ISSN:
0006-3525
URN:
uuid:b0125234-0ade-4761-839e-e68f3a634912
Source identifiers:
100554
Local pid:
pubs:100554

Terms of use


Metrics


Views and Downloads






If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP