By smaller peptide I mean somewhere around 15-20 aminoacids, having a cycle or two that constrain the geometry.
Also - I am interested in getting as much detail about the structure of the peptide as possible.
Do you typically need to record NOE buildup curves in such cases?
Given that side-chains of the peptide are unlikely to be packed like in the core of the globular protein - do you include side-chain NOE's into structure calculations?
Could you recommend any citations?
Thank you!.
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[NMR paper] NMR solution structure of a peptide from the mdm-2 binding domain of the p53 protein
NMR solution structure of a peptide from the mdm-2 binding domain of the p53 protein that is selectively cytotoxic to cancer cells.
Related Articles NMR solution structure of a peptide from the mdm-2 binding domain of the p53 protein that is selectively cytotoxic to cancer cells.
Biochemistry. 2004 Feb 24;43(7):1854-61
Authors: Rosal R, Pincus MR, Brandt-Rauf PW, Fine RL, Michl J, Wang H
We have recently found that a peptide from the mdm-2 binding domain of the p53 protein induced rapid membranolytic necrosis of a variety of different human...
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11-24-2010 09:25 PM
[NMR paper] Influence of pH on NMR structure and stability of the human prion protein globular do
Influence of pH on NMR structure and stability of the human prion protein globular domain.
Related Articles Influence of pH on NMR structure and stability of the human prion protein globular domain.
J Biol Chem. 2003 Sep 12;278(37):35592-6
Authors: Calzolai L, Zahn R
The NMR structure of the globular domain of the human prion protein (hPrP) with residues 121-230 at pH 7.0 shows the same global fold as the previously published structure determined at pH 4.5. It contains three alpha-helices, comprising residues 144-156, 174-194, and 200-228, and...
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11-24-2010 09:01 PM
[NMR paper] The structure and dipole moment of globular proteins in solution and crystalline stat
The structure and dipole moment of globular proteins in solution and crystalline states: use of NMR and X-ray databases for the numerical calculation of dipole moment.
Related Articles The structure and dipole moment of globular proteins in solution and crystalline states: use of NMR and X-ray databases for the numerical calculation of dipole moment.
Biopolymers. 2001 Apr 5;58(4):398-409
Authors: Takashima S
The large dipole moment of globular proteins has been well known because of the detailed studies using dielectric relaxation and...
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11-19-2010 08:32 PM
[NMR paper] Thermal stability studies of a globular protein in aqueous poly(ethylene glycol) by (
Thermal stability studies of a globular protein in aqueous poly(ethylene glycol) by (1)H NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_120x27.gif Related Articles Thermal stability studies of a globular protein in aqueous poly(ethylene glycol) by (1)H NMR.
Biotechnol Bioeng. 1996 Aug 20;51(4):410-21
Authors: Hancock TJ, Hsu JT
The reversible folding destabilization of hen lysozyme has been confirmed by a melting temperature (T(m)) decrease in aqueous...
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08-22-2010 02:20 PM
[NMR paper] Crystal structure of the SH2 domain from the adaptor protein SHC: a model for peptide
Crystal structure of the SH2 domain from the adaptor protein SHC: a model for peptide binding based on X-ray and NMR data.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Crystal structure of the SH2 domain from the adaptor protein SHC: a model for peptide binding based on X-ray and NMR data.
J Mol Biol. 1995 Nov 17;254(1):86-95
Authors: Mikol V, Baumann G, Zurini MG, Hommel U
Src homology 2 domains (SH2) are protein molecules found within a wide variety of cytoplasmic...
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08-22-2010 03:50 AM
[NMR paper] NMR structure of a receptor-bound G-protein peptide.
NMR structure of a receptor-bound G-protein peptide.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.nature.com-images-lo_nature.gif Related Articles NMR structure of a receptor-bound G-protein peptide.
Nature. 1993 May 20;363(6426):276-81
Authors: Dratz EA, Furstenau JE, Lambert CG, Thireault DL, Rarick H, Schepers T, Pakhlevaniants S, Hamm HE
Heterotrimeric GTP-binding proteins (G proteins) regulate cellular activity by coupling to hormone or sensory receptors. Stimulated receptors catalyse the release of GDP from G protein...
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08-21-2010 11:53 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...