Simulations of the c-subunit of ATP-synthase reveal helix rearrangements.
about
Conformational flexibility of the leucine binding protein examined by protein domain coarse-grained molecular dynamics.Release of content through mechano-sensitive gates in pressurized liposomes.The energetics of transmembrane helix insertion into a lipid bilayer.The Phylogenetic Signature Underlying ATP Synthase c-Ring Compliance.Cholesterol modulates the dimer interface of the β₂-adrenergic receptor via cholesterol occupancy sites.Perspective on the Martini model.Immobilization of the plug domain inside the SecY channel allows unrestricted protein translocation.Sequence dependent lipid-mediated effects modulate the dimerization of ErbB2 and its associative mutants.
P2860
Q30353714-6F569293-A855-4778-B2AD-4E2ADBB5EAB5Q34147450-F76C4F52-ADEB-41B1-A3DD-34EB7EE0AB0EQ34202203-C627327E-DB56-4505-AD8E-A962288C7A4AQ36043811-65CDFDFD-AA8B-43EE-B60C-9EDF66181114Q37700209-8DC3624C-4E47-42F9-9E21-23F9B9AEBAC2Q38109488-035372B4-D541-46E4-B5C5-C3B71DA4F3DCQ41936753-690447B2-F234-4B78-B84F-A0435DAF2AF8Q45337419-6216A27F-96C5-454E-A3FA-B13A82389EAB
P2860
Simulations of the c-subunit of ATP-synthase reveal helix rearrangements.
description
2009 nî lūn-bûn
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2009年の論文
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2009年学术文章
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2009年学术文章
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2009年学术文章
@zh-hans
2009年学术文章
@zh-my
2009年学术文章
@zh-sg
2009年學術文章
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2009年學術文章
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2009年學術文章
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name
Simulations of the c-subunit of ATP-synthase reveal helix rearrangements.
@en
Simulations of the c-subunit of ATP-synthase reveal helix rearrangements.
@nl
type
label
Simulations of the c-subunit of ATP-synthase reveal helix rearrangements.
@en
Simulations of the c-subunit of ATP-synthase reveal helix rearrangements.
@nl
prefLabel
Simulations of the c-subunit of ATP-synthase reveal helix rearrangements.
@en
Simulations of the c-subunit of ATP-synthase reveal helix rearrangements.
@nl
P2860
P1476
Simulations of the c-subunit of ATP-synthase reveal helix rearrangements.
@en
P2093
Aldo Rampioni
Siewert-Jan Marrink
P2860
P304
P356
10.3109/09687680903321073
P577
2009-12-01T00:00:00Z