NMR paper Conformation of parathyroid hormone antagonists by CD, NMR, and molecular dynamics si

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[NMR paper] Conformation of parathyroid hormone antagonists by CD, NMR, and molecular dynamics si

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NMR processing:

MDD

NMR assignment:

Backbone:

Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

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GeNMR

I-TASSER

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Amber

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Torsion angles from chemical shifts:

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TALOS

Promega- Proline

Secondary structure from chemical shifts:

CSI (via RCI server)

TALOS

MICS caps, β-turns

d2D

PECAN

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RCI

Interactions from chemical shifts:

HADDOCK

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B-factor

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ArShift- Aromatic

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Camcoil

Poulsen_rc_CS

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Conformation of parathyroid hormone antagonists by CD, NMR, and molecular dynamics si

Conformation of parathyroid hormone antagonists by CD, NMR, and molecular dynamics simulations.

Related Articles Conformation of parathyroid hormone antagonists by CD, NMR, and molecular dynamics simulations.

Biopolymers. 1995 Oct;36(4):485-95

Authors: Chorev M, Behar V, Yang Q, Rosenblatt M, Mammi S, Maretto S, Pellegrini M, Peggion E

The conformation of two highly potent parathyroid hormone (PTH) antagonists was investigated in water/2,2,2-trifluoroethanol mixtures. The two peptides are derived from the sequence (7-34) of PTH and of PTH-related protein (PTHrP) and have a D-Trp replacing Gly in position 12. In the analogue derived from PTHrP, Lys11 was replaced by Leu to remove the residual agonist activity. The study was conducted by CD and two-dimensional proton magnetic resonance spectroscopy, and the nuclear Overhauser effects found were utilized in restrained distance geometry and molecular dynamics simulations. Both peptides adopt a helical C-terminal conformation, which seems more stable in the case of the PTHrP analogue. A type II' beta-turn centered around D-Trp12 and Lys13 is present in both structures.

PMID: 7578943 [PubMed - indexed for MEDLINE]

Source: PubMed

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