Related ArticlesConformational analysis of peptide analogues of silkmoth chorion protein segments using CD, NMR and molecular modelling.
J Pept Sci. 2004 Jun;10(6):381-92
Authors: Benaki DC, Mikros E, Hamodrakas SJ
Silkmoth proteins secreted from the follicular cells that surround the oocyte form a large extracellular assembly which is important for protecting and sustaining the structure of the oocyte and the developing embryo. These proteins have been classified into two major families (A and B). Sequence analysis showed conservation of a central domain containing long stretches of six amino acid residue repeats in both families, which have been suggested to be organized in beta-sheet structures. In this work NMR and CD spectra, as well as molecular calculations, have been used to investigate the conformational properties of two synthetic peptides (A and B), analogues of parts of the central domain of silkmoth chorion proteins of the A and B families, respectively. These peptides consist of three tandem repeats of the six-residue basic motif. Analysis of CD spectra of the two peptides in aqueous solutions and mixtures with organic solvents revealed beta-sheet and turn structural elements with a percentage higher than 40%. NOESY spectra at low temperatures (263-273 K) show sequential nOe connectivities (i, i + 1), indicative of a relative flexibility. The presence of HNi-HNi+1 cross-peaks and medium Halphai-HNi+1 connectivities, chemical shift deviations and temperature coefficient data provide, for the first time, experimental evidence that local folded structures around Gly residues occur in peptide segments of chorion proteins in solution. Simulated annealing calculations were used to examine the conformational space of the peptides and to probe the initial steps of amyloid fibril formation in the case of chorion proteins.
[NMR paper] Magic-angle spinning solid-state NMR spectroscopy of the beta1 immunoglobulin binding domain of protein G (GB1): 15N and 13C chemical shift assignments and conformational analysis.
Magic-angle spinning solid-state NMR spectroscopy of the beta1 immunoglobulin binding domain of protein G (GB1): 15N and 13C chemical shift assignments and conformational analysis.
Related Articles Magic-angle spinning solid-state NMR spectroscopy of the beta1 immunoglobulin binding domain of protein G (GB1): 15N and 13C chemical shift assignments and conformational analysis.
J Am Chem Soc. 2005 Sep 7;127(35):12291-305
Authors: Franks WT, Zhou DH, Wylie BJ, Money BG, Graesser DT, Frericks HL, Sahota G, Rienstra CM
Magic-angle spinning...
nmrlearner
Journal club
0
12-01-2010 06:56 PM
[NMR paper] Protein energetic conformational analysis from NMR chemical shifts (PECAN) and its us
Protein energetic conformational analysis from NMR chemical shifts (PECAN) and its use in determining secondary structural elements.
Related Articles Protein energetic conformational analysis from NMR chemical shifts (PECAN) and its use in determining secondary structural elements.
J Biomol NMR. 2005 May;32(1):71-81
Authors: Eghbalnia HR, Wang L, Bahrami A, Assadi A, Markley JL
We present an energy model that combines information from the amino acid sequence of a protein and available NMR chemical shifts for the purposes of identifying low...
nmrlearner
Journal club
0
11-25-2010 08:21 PM
[NMR paper] Conformational analysis by NMR and distance geometry techniques of a peptide mimetic
Conformational analysis by NMR and distance geometry techniques of a peptide mimetic of the third helix of the Antennapedia homeodomain.
Related Articles Conformational analysis by NMR and distance geometry techniques of a peptide mimetic of the third helix of the Antennapedia homeodomain.
J Pept Res. 2005 Feb;65(2):200-8
Authors: Saviano M, Isernia C, Bassarello C, Di Lello P, Galdiero S, Mierke DF, Benedetti E, Pedone C
The Antennapedia homeodomain structure consists of four helices. The helices II and III are connected by a tripeptide that...
nmrlearner
Journal club
0
11-24-2010 11:14 PM
[NMR paper] NMR observation of selected segments in a larger protein: central-segment isotope lab
NMR observation of selected segments in a larger protein: central-segment isotope labeling through intein-mediated ligation.
Related Articles NMR observation of selected segments in a larger protein: central-segment isotope labeling through intein-mediated ligation.
Biochemistry. 1999 Dec 7;38(49):16040-4
Authors: Otomo T, Ito N, Kyogoku Y, Yamazaki T
Peptide segments in a protein, which can include an active site of interest or be a series of parts constituting the entire structure, are now selectively observed by nuclear magnetic resonance...
nmrlearner
Journal club
0
11-18-2010 08:31 PM
[NMR paper] Structure of segments of a G protein-coupled receptor: CD and NMR analysis of the Sac
Structure of segments of a G protein-coupled receptor: CD and NMR analysis of the Saccharomyces cerevisiae tridecapeptide pheromone receptor.
Related Articles Structure of segments of a G protein-coupled receptor: CD and NMR analysis of the Saccharomyces cerevisiae tridecapeptide pheromone receptor.
Biopolymers. 1998 Nov;46(6):343-57
Authors: Arshava B, Liu SF, Jiang H, Breslav M, Becker JM, Naider F
Peptides representing both loop and the sixth transmembrane regions of the alpha-factor receptor of Saccharomyces cerevisiae were synthesized by...
nmrlearner
Journal club
0
11-17-2010 11:15 PM
[NMR paper] Conformational analysis of protein structures derived from NMR data.
Conformational analysis of protein structures derived from NMR data.
Related Articles Conformational analysis of protein structures derived from NMR data.
Proteins. 1993 Nov;17(3):232-51
Authors: MacArthur MW, Thornton JM
A study is presented of the conformational characteristics of NMR-derived protein structures in the Protein Data Bank compared to X-ray structures. Both ensemble and energy-minimized average structures are analyzed. We have addressed the problem using the methods developed for crystal structures by examining the distribution...
nmrlearner
Journal club
0
08-22-2010 03:01 AM
[NMR paper] Analysis of side-chain conformational distributions in neutrophil peptide-5 NMR struc
Analysis of side-chain conformational distributions in neutrophil peptide-5 NMR structures.
Related Articles Analysis of side-chain conformational distributions in neutrophil peptide-5 NMR structures.
Biopolymers. 1990 Dec;29(14):1807-22
Authors: Kominos D, Bassolino DA, Levy RM, Pardi A
The side-chain conformations have been analyzed in the antimicrobial peptide, Neutrophil Peptide-5 (NP-5), whose structure was independently generated from nmr-derived distance constraints using a distance geometry algorithm. The side-chain and peptide...
nmrlearner
Journal club
0
08-21-2010 11:04 PM
Analysis of NMR Chemical Shifts in Peptide & Protein Structure Determination-Wang '08
Analysis of NMR Chemical Shifts in Peptide and Protein Structure Determination
By Liya Wang (2008)
Amazon book description
Chemical shifts provide detailed information about non-covalent structure, solvent interactions, ionization constants, ring orientations, hydrogen bond interactions, and other phenomena. Since different chemical shift data sets are not necessarily comparable without corrections or adjustments, the applicability of statistical analysis of NMR chemical shifts to biomolecules has so far been limited. We use the term "congruent" to describe data sets that can be...
Conformational analysis of peptide analogues of silkmoth chorion protein segments usi
Linear Mode
