NMR paper Structural study of caveolin-1 intramembrane domain by CD and NMR.

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[NMR paper] Structural study of caveolin-1 intramembrane domain by CD and NMR.

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NMR processing:

MDD

NMR assignment:

Backbone:

Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

Template-based:

GeNMR

I-TASSER

Refinement:

Amber

Structure from chemical shifts:

Fragment-based:

Homology-based:

Torsion angles from chemical shifts:

Preditor

TALOS

Promega- Proline

Secondary structure from chemical shifts:

CSI (via RCI server)

TALOS

MICS caps, β-turns

d2D

PECAN

Flexibility from chemical shifts:

RCI

Interactions from chemical shifts:

HADDOCK

Chemical shifts re-referencing:

NMR model quality:

NOEs, other restraints:

Chemical shifts:

RDCs:

Pseudocontact shifts:

Protein geomtery:

SAVES2 or SAVES4

Quality Control Check

NMR spectrum prediction:

FANDAS

MestReS

V-NMR

Flexibility from structure:

Backbone S2

Methyl S2

B-factor

Molecular dynamics:

Gromacs

Amber

Antechamber

Chemical shifts prediction:

From structure:

Shiftx2

Sparta+

Camshift

CH3shift- Methyl

ArShift- Aromatic

ShiftS

Proshift

PPM

CheShift-2- Cα

From sequence:

Shifty

Camcoil

Poulsen_rc_CS

Disordered proteins:

MAXOCC

Format conversion & validation:

CCPN

From NMR-STAR 3.1

Validate NMR-STAR 3.1

NMR sample preparation:

Protein disorder:

DisMeta

Protein solubility:

Isotope labeling:

Solid-state NMR:

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12-06-2014, 04:54 AM

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Structural study of caveolin-1 intramembrane domain by CD and NMR.

Related Articles Structural study of caveolin-1 intramembrane domain by CD and NMR.

Biopolymers. 2014 Dec 4;

Authors: Yang G, Dong Z, Xu H, Wang C, Li H, Li Z, Li F

Abstract
Caveolin-1 is a main structural component of caveolae and essential for the invagination of caveolae by forming a hairpin structure in the membrane-inserting domain (residues 102-122). In the present paper, we determined the tertiary structures of the peptides comprising residues 93-126 and 101-126 of caveolin-1in 1,1,1,3,3,3-hexafluoro-2-propanol (HFIP) aqueous solution and sodium dodecyl sulfate (SDS) micelles, respectively, by NMR study. The self-association of the peptides in SDS and dodecylphosphocholine (DPC) micelles was also studied by CD, NMR and SDS-PAGE techniques. Our results indicated that both peptides form a helix-break-helix structure with two helices spanning over Leu103-Phe107 and Ile117-His126 and a loop ranging over Gly108-Gly116. The addition of the segment Thr93-Arg101 to the N-terminal end of the intramembrane domain promoted more oligomerization of the peptide 93-126 than the peptide 101-126 in the micelles. Our results suggested that the glycine residues at position 108 and 116 are important for the break of the helical structure of the membrane-inserting domain and the segment Thr93-Arg101 flanking the membrane-inserting domain may play a role in the self-association of the caveolin-1 protein at cellular membrane. This article is protected by copyright. All rights reserved.

PMID: 25471446 [PubMed - as supplied by publisher]

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