Related ArticlesThe cisproline(i - 1)-aromatic(i) interaction: folding of the Ala-cisPro-Tyr peptide characterized by NMR and theoretical approaches.
J Biomol NMR. 2000 May;17(1):63-77
Authors: Nardi F, Kemmink J, Sattler M, Wade RC
Cisproline(i - 1)-aromatic(i) interactions have been detected in several short peptides in aqueous solution by analysis of anomalous chemical shifts measured by 1H-NMR spectroscopy. This formation of local structure is of importance for protein folding and binding properties. To obtain an atomic-detail characterisation of the cisproline(i - 1)-aromatic(i) interaction in terms of structure, energetics and dynamics, we studied the minimal peptide unit, blocked Ala-cisPro-Tyr, using computational and experimental techniques. Structural database analyses and a systematic search revealed two groups of conformations displaying a cisproline(i - 1)-aromatic(i) interaction. These conformations were taken as seeds for molecular dynamics simulations in explicit solvent at 278 K. During a total of 33.6 ns of simulation, all the 'folded' conformations and some 'unfolded' states were sampled. 1H- and 13C-chemical shifts and 3J-coupling constants were measured for the Ala-Pro-Tyr peptide. Excellent agreement was found between all the measured and computed NMR properties, showing the good quality of the force field. We find that under the experimental and simulation conditions, the Ala-cisPro-Tyr peptide is folded 90% of the time and displays two types of folded conformation which we denote 'a' and 'b'. The type a conformations are twice as populated as the type b conformations. The former have the tyrosine ring interacting with the alanine alpha proton and are enthalpically stabilised. The latter have the aromatic ring interacting with the proline side chain and are entropically stabilised. The combined and complementary use of computational and experimental techniques permitted derivation of a detailed scenario of the 'folding' of this peptide.
[Question from NMRWiki Q&A forum] peptide protein interaction
peptide protein interaction
I have determined the structure of a 110 residues protein(11kDa) which is known to interact with a 15mer peptide. Now I am interested to know which residues of the 15mer peptide interacts with this 11kDa protein. Can anyone suggest a simple nmr experiment which can tell the residues from the 15mer peptide which interact with the protein.
Check if somebody has answered this question on NMRWiki QA forum
[NMR paper] Interaction of the fusogenic peptide B18 in its amyloid-state with lipid membranes st
Interaction of the fusogenic peptide B18 in its amyloid-state with lipid membranes studied by solid state NMR.
Related Articles Interaction of the fusogenic peptide B18 in its amyloid-state with lipid membranes studied by solid state NMR.
Chem Phys Lipids. 2004 Nov;132(1):65-77
Authors: Grage SL, Afonin S, Grüne M, Ulrich AS
The interaction of the fusogenic polypeptide segment "B18" from the fertilization protein binding with lipid membranes was investigated by solid state 2H and 31P NMR, and by differential scanning calorimetry. B18 is known...
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11-24-2010 10:03 PM
[NMR paper] Membrane position of a basic aromatic peptide that sequesters phosphatidylinositol 4,
Membrane position of a basic aromatic peptide that sequesters phosphatidylinositol 4,5 bisphosphate determined by site-directed spin labeling and high-resolution NMR.
Related Articles Membrane position of a basic aromatic peptide that sequesters phosphatidylinositol 4,5 bisphosphate determined by site-directed spin labeling and high-resolution NMR.
Biophys J. 2004 Nov;87(5):3221-33
Authors: Ellena JF, Moulthrop J, Wu J, Rauch M, Jaysinghne S, Castle JD, Cafiso DS
The membrane interactions and position of a positively charged and highly...
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[NMR paper] NMR study on the interaction between MHC class I protein and its antigen peptide.
NMR study on the interaction between MHC class I protein and its antigen peptide.
Related Articles NMR study on the interaction between MHC class I protein and its antigen peptide.
Biochem Biophys Res Commun. 2000 Nov 30;278(3):609-13
Authors: Nakagawa M, Chiba-Kamoshida K, Udaka K, Nakanishi H
A major histcompatibility complex (MHC) class I protein H-2K(b) was expressed in a large scale as a fusion protein with thioredoxin and hexahistidine at the N-terminus to analyze the interaction with the antigen peptide SIYRYYGL. NMR spectra of the...
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[NMR paper] NMR behavior of the aromatic protons of bovine neurophysin-I and its peptide complexe
NMR behavior of the aromatic protons of bovine neurophysin-I and its peptide complexes: implications for solution structure and for function.
Related Articles NMR behavior of the aromatic protons of bovine neurophysin-I and its peptide complexes: implications for solution structure and for function.
Biochemistry. 1995 Feb 21;34(7):2137-47
Authors: Breslow E, Sardana V, Deeb R, Barbar E, Peyton DH
The NMR behavior of the aromatic protons of bovine neurophysin-I and its complexes was interpreted with reference to the 2.8 A crystal structure of...
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[Question from NMRWiki Q&A forum] NMR experiments to assign aromatic sidechains?
NMR experiments to assign aromatic sidechains?
Hello, may I ask this - NMR experiments/pulse sequences are available to assign aromatic sidechains - Phe, Tyr, Trp? We'd like to try 2D and 3D.
What's available in the vendor-specific libraries?
Thank you very much.
The cisproline(i - 1)-aromatic(i) interaction: folding of the Ala-cisPro-Tyr peptide
Linear Mode
