NMR paper Protein-chromophore interactions in alpha-crustacyanin, the major blue carotenoprotei

		BioNMR > Educational resources > Journal club
[NMR paper] Protein-chromophore interactions in alpha-crustacyanin, the major blue carotenoprotei

Webservers

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:

Thread Tools

Search this Thread

Rate Thread

Display Modes

08-22-2010, 03:41 AM

nmrlearner

Senior Member

Join Date: Jan 2005

Posts: 23,700

Points: 193,617, Level: 100

Level up: 0%, 0 Points needed

Activity: 50.7%

Last Achievements

Award-Showcase

NMR Credits: 0

NMR Points: 193,617

Downloads: 0

Uploads: 0

Protein-chromophore interactions in alpha-crustacyanin, the major blue carotenoprotei

Protein-chromophore interactions in alpha-crustacyanin, the major blue carotenoprotein from the carapace of the lobster, Homarus gammarus. A study by 13C magic angle spinning NMR.

Related Articles Protein-chromophore interactions in alpha-crustacyanin, the major blue carotenoprotein from the carapace of the lobster, Homarus gammarus. A study by 13C magic angle spinning NMR.

FEBS Lett. 1995 Mar 27;362(1):34-8

Authors: Weesie RJ, Askin D, Jansen FJ, de Groot HJ, Lugtenburg J, Britton G

MAS (magic angle spinning) 13C NMR has been used to study protein-chromophore interactions in alpha-crustacyanin, the blue astaxanthin-binding carotenoprotein of the lobster, Homarus gammarus, reconstituted with astaxanthins labelled with 13C at the 14,14' or 15,15' positions. Two signals are seen for alpha-crustacyanin containing [14,14'-13C2]astaxanthin, shifted 6.9 and 4.0 ppm downfield from the 134.1 ppm signal of uncomplexed astaxanthin in the solid state. With alpha-crustacyanin containing [15,15'-13C2]astaxanthin, one essentially unshifted broad signal is seen. Hence binding to the protein causes a decrease in electronic charge density, providing the first experimental evidence that a charge redistribution mechanism contributes to the bathochromic shift of the astaxanthin in alpha-crustacyanin, in agreement with inferences based on resonance Raman data [Salares, et al. (1979) Biochim. Biophys. Acta 576, 176-191]. The splitting of the 14 and 14' signals provides evidence for asymmetric binding of each astaxanthin molecule by the protein.

PMID: 7698348 [PubMed - indexed for MEDLINE]

Source: PubMed

Did you find this post helpful?

Similar Threads
Thread	Thread Starter	Forum	Replies	Last Post
[NMR paper] Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble molecular dynamics simulations. Related Articles Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble molecular dynamics simulations. J Am Chem Soc. 2005 Jan 19;127(2):476-7 Authors: Dedmon MM, Lindorff-Larsen K, Christodoulou J, Vendruscolo M, Dobson CM The intrinsically disordered protein alpha-synuclein plays a key role in the pathogenesis of Parkinson's disease (PD). We show here that the native state of alpha-synuclein...	nmrlearner	Journal club	0	11-24-2010 11:14 PM
[NMR paper] Dissecting structural and electrostatic interactions of charged groups in alpha-sarci Dissecting structural and electrostatic interactions of charged groups in alpha-sarcin. An NMR study of some mutants involving the catalytic residues. Related Articles Dissecting structural and electrostatic interactions of charged groups in alpha-sarcin. An NMR study of some mutants involving the catalytic residues. Biochemistry. 2003 Nov 18;42(45):13122-33 Authors: García-Mayoral MF, Pérez-Cañadillas JM, Santoro J, Ibarra-Molero B, Sanchez-Ruiz JM, Lacadena J, Martínez del Pozo A, Gavilanes JG, Rico M, Bruix M The cytotoxic ribonuclease...	nmrlearner	Journal club	0	11-24-2010 09:16 PM
[NMR paper] Metal-ligand interactions in perturbed blue copper sites: a paramagnetic (1)H NMR stu Metal-ligand interactions in perturbed blue copper sites: a paramagnetic (1)H NMR study of Co(II)-pseudoazurin. Related Articles Metal-ligand interactions in perturbed blue copper sites: a paramagnetic (1)H NMR study of Co(II)-pseudoazurin. J Biol Inorg Chem. 2003 Jan;8(1-2):75-82 Authors: Fernández CO, Niizeki T, Kohzuma T, Vila AJ Pseudoazurin is an electron transfer copper protein, a member of the cupredoxin family. The protein is frequently found in denitrifying bacteria, where it is the electron donor of nitrite reductase. The copper at...	nmrlearner	Journal club	0	11-24-2010 08:58 PM
[NMR paper] Electronic characterization of the oxidized state of the blue copper protein rusticya Electronic characterization of the oxidized state of the blue copper protein rusticyanin by 1H NMR: is the axial methionine the dominant influence for the high redox potential? Related Articles Electronic characterization of the oxidized state of the blue copper protein rusticyanin by 1H NMR: is the axial methionine the dominant influence for the high redox potential? Biochemistry. 2001 Jan 23;40(3):837-46 Authors: Donaire A, Jiménez B, Moratal J, Hall JF, Hasnain SS The oxidized state of rusticyanin, the blue copper protein with the highest...	nmrlearner	Journal club	0	11-19-2010 08:32 PM
[NMR paper] Electrostatic interactions in the acid denaturation of alpha-lactalbumin determined b Electrostatic interactions in the acid denaturation of alpha-lactalbumin determined by NMR. Related Articles Electrostatic interactions in the acid denaturation of alpha-lactalbumin determined by NMR. Protein Sci. 1998 Sep;7(9):1930-8 Authors: Kim S, Baum J alpha-Lactalbumin (alpha-LA) undergoes a pH-dependent unfolding from the native state to a partially unfolded state (the molten globule state). To understand the role of electrostatic interactions in protein denaturation, NMR and CD pH titration experiments are performed on guinea pig...	nmrlearner	Journal club	0	11-17-2010 11:15 PM
[NMR paper] NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and c NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and chaperone action of small heat-shock proteins. Related Articles NMR spectroscopy of alpha-crystallin. Insights into the structure, interactions and chaperone action of small heat-shock proteins. Int J Biol Macromol. 1998 May-Jun;22(3-4):197-209 Authors: Carver JA, Lindner RA The subunit molecular mass of alpha-crystallin, like many small heat-shock proteins (sHsps), is around 20 kDa although the protein exists as a large aggregate of average mass around 800...	nmrlearner	Journal club	0	11-17-2010 11:06 PM
[NMR paper] 1H-NMR study of a cobalt-substituted blue copper protein: Pseudomonas aeruginosa Co(I 1H-NMR study of a cobalt-substituted blue copper protein: Pseudomonas aeruginosa Co(II)-azurin. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles 1H-NMR study of a cobalt-substituted blue copper protein: Pseudomonas aeruginosa Co(II)-azurin. Eur J Biochem. 1995 Jul 15;231(2):358-69 Authors: Salgado J, JimÃ©nez HR, Donaire A, Moratal JM Substitution of copper by cobalt in blue copper proteins gives a paramagnetic metalloderivative...	nmrlearner	Journal club	0	08-22-2010 03:50 AM
[NMR paper] A NMR investigation on the interactions of the alpha-oligomeric form of the M13 coat A NMR investigation on the interactions of the alpha-oligomeric form of the M13 coat protein with lipids, which mimic the Escherichia coli inner membrane. http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles A NMR investigation on the interactions of the alpha-oligomeric form of the M13 coat protein with lipids, which mimic the Escherichia coli inner membrane. Biochim Biophys Acta. 1991 Jul 1;1066(1):102-8 Authors: Sanders JC, Poile TW, Spruijt RB, Van Nuland NA, Watts A, Hemminga MA ...	nmrlearner	Journal club	0	08-21-2010 11:16 PM

« Previous Thread | Next Thread »

Posting Rules
You may not post new threads You may not post replies You may not post attachments You may not edit your posts BB code is On Smilies are On [IMG] code is On HTML code is On Trackbacks are Off Pingbacks are Off Refbacks are Off