Related Articles1H NMR structure of an antifungal gamma-thionin protein SIalpha1: similarity to scorpion toxins.
Proteins. 1998 Aug 15;32(3):334-49
Authors: Bloch C, Patel SU, Baud F, Zvelebil MJ, Carr MD, Sadler PJ, Thornton JM
The three-dimensional structure of the Sorghum bicolor seed protein gamma-thionin SIalpha1 has been determined by 2D 1H nuclear magnetic resonance (NMR) spectroscopy. The secondary structure of this 47-residue antifungal protein with four disulphide bridges consists of a three-stranded antiparallel sheet and one helix. The helix is tethered to the sheet by two disulphide bridges which link two successive turns of the helix to alternate residues i, i+2 in one strand. Possible binding sites for antifungal activity are discussed. The same fold has been observed previously in several scorpion toxins.
[NMR paper] Study of the conformation of gamma-zeins in purified maize protein bodies by FTIR and NMR spectroscopy.
Study of the conformation of gamma-zeins in purified maize protein bodies by FTIR and NMR spectroscopy.
Related Articles Study of the conformation of gamma-zeins in purified maize protein bodies by FTIR and NMR spectroscopy.
Anal Bioanal Chem. 2005 Sep;383(2):291-6
Authors: Bicudo TC, Forato LA, Batista LA, Colnago LA
The gamma-zeins are a mixture of 16, 27, and 50-kDa polypeptides which are important in the formation and stabilization of protein bodies (PB). These organelles are used for deposition of zeins, the water-insoluble storage...
nmrlearner
Journal club
0
12-01-2010 06:56 PM
[NMR paper] NMR solution structure of hPar14 reveals similarity to the peptidyl prolyl cis/trans
NMR solution structure of hPar14 reveals similarity to the peptidyl prolyl cis/trans isomerase domain of the mitotic regulator hPin1 but indicates a different functionality of the protein.
Related Articles NMR solution structure of hPar14 reveals similarity to the peptidyl prolyl cis/trans isomerase domain of the mitotic regulator hPin1 but indicates a different functionality of the protein.
J Mol Biol. 2000 Aug 25;301(4):1003-17
Authors: Sekerina E, Rahfeld JU, Müller J, Fanghänel J, Rascher C, Fischer G, Bayer P
The 131-amino acid residue...
nmrlearner
Journal club
0
11-19-2010 08:29 PM
[NMR paper] NMR structure of a protein kinase C-gamma phorbol-binding domain and study of protein
NMR structure of a protein kinase C-gamma phorbol-binding domain and study of protein-lipid micelle interactions.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles NMR structure of a protein kinase C-gamma phorbol-binding domain and study of protein-lipid micelle interactions.
Biochemistry. 1997 Sep 2;36(35):10709-17
Authors: Xu RX, Pawelczyk T, Xia TH, Brown SC
Classical protein kinase C (PKC) family members are activated by the binding of various ligands to one of several cysteine-rich...
nmrlearner
Journal club
0
08-22-2010 05:08 PM
[NMR paper] Refinement of the NMR solution structure of the gamma-carboxyglutamic acid domain of
Refinement of the NMR solution structure of the gamma-carboxyglutamic acid domain of coagulation factor IX using molecular dynamics simulation with initial Ca2+ positions determined by a genetic algorithm.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Refinement of the NMR solution structure of the gamma-carboxyglutamic acid domain of coagulation factor IX using molecular dynamics simulation with initial Ca2+ positions determined by a genetic algorithm.
Biochemistry. 1997 Feb 25;36(8):2132-8
...
nmrlearner
Journal club
0
08-22-2010 03:31 PM
[NMR paper] Refinement of the NMR solution structure of the gamma-carboxyglutamic acid domain of
Refinement of the NMR solution structure of the gamma-carboxyglutamic acid domain of coagulation factor IX using molecular dynamics simulation with initial Ca2+ positions determined by a genetic algorithm.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Refinement of the NMR solution structure of the gamma-carboxyglutamic acid domain of coagulation factor IX using molecular dynamics simulation with initial Ca2+ positions determined by a genetic algorithm.
Biochemistry. 1997 Feb 25;36(8):2132-8
...
[NMR paper] Structure of the metal-free gamma-carboxyglutamic acid-rich membrane binding region o
Structure of the metal-free gamma-carboxyglutamic acid-rich membrane binding region of factor IX by two-dimensional NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles Structure of the metal-free gamma-carboxyglutamic acid-rich membrane binding region of factor IX by two-dimensional NMR spectroscopy.
J Biol Chem. 1995 Apr 7;270(14):7980-7
Authors: Freedman SJ, Furie BC, Furie B, Baleja JD
The gamma-carboxyglutamic acid-rich...
nmrlearner
Journal club
0
08-22-2010 03:41 AM
[NMR paper] NMR solution structure of the antifungal protein from Aspergillus giganteus: evidence
NMR solution structure of the antifungal protein from Aspergillus giganteus: evidence for cysteine pairing isomerism.
Related Articles NMR solution structure of the antifungal protein from Aspergillus giganteus: evidence for cysteine pairing isomerism.
Biochemistry. 1995 Mar 7;34(9):3009-21
Authors: Campos-Olivas R, Bruix M, Santoro J, Lacadena J, Martinez del Pozo A, Gavilanes JG, Rico M
The solution structure of the antifungal protein (AFP, 51 residues, 4 disulfide bridges) from Aspergillus giganteus has been determined by using...
1H NMR structure of an antifungal gamma-thionin protein SIalpha1: similarity to scorp
Linear Mode
