Related Articles1H NMR studies of the mercuric ion binding protein MerP: sequential assignment, secondary structure and global fold of oxidized MerP.
J Biomol NMR. 1993 Nov;3(6):613-26
Authors: Eriksson PO, Sahlman L
The oxidized form of the mercuric ion binding protein MerP has been studied by two-dimensional NMR. MerP, which is a periplasmic water-soluble protein with 72 amino acids, is involved in the detoxification of mercuric ions in bacteria with resistance against mercury. The mercuric ions in the periplasmic space are first scavenged by the MerP protein, then transported into the cytoplasm by the membrane-bound transport protein MerT, and finally reduced to elementary (nontoxic) mercury by the enzyme mercuric reductase. In this work, the 1H NMR spectrum of oxidized MerP (closed disulfide bridge) has been assigned by using homonuclear 2D NMR techniques. The secondary structure and global fold have been inferred from the nuclear Overhauser effect (NOE) data. The secondary structure comprises four beta-strands and two alpha-helices, in the order beta 1 alpha 1 beta 2 beta 3 alpha 2 beta 4. The protein folds into an antiparallel beta-sheet, beta 2 beta 3 beta 1 beta 4, with the two antiparallel helices on one side of the sheet. The folding topology is similar to that of acylphosphatase, the activation domain of porcine pancreatic procarboxypeptidase B, the DNA-binding domain of bovine papillomavirus-1 E2 and the RNA-binding domains of the U1 snRNP A and hnRNP C proteins. However, there is no structural similarity between MerP and other bacterial periplasmic binding proteins.
[NMR paper] A random graph approach to NMR sequential assignment.
A random graph approach to NMR sequential assignment.
Related Articles A random graph approach to NMR sequential assignment.
J Comput Biol. 2005 Jul-Aug;12(6):569-83
Authors: Bailey-Kellogg C, Chainraj S, Pandurangan G
Nuclear magnetic resonance (NMR) spectroscopy allows scientists to study protein structure, dynamics and interactions in solution. A necessary first step for such applications is determining the resonance assignment, mapping spectral data to atoms and residues in the primary sequence. Automated resonance assignment algorithms...
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[NMR paper] A sequential HNCA NMR pulse sequence for protein backbone assignment.
A sequential HNCA NMR pulse sequence for protein backbone assignment.
Related Articles A sequential HNCA NMR pulse sequence for protein backbone assignment.
J Magn Reson. 2001 May;150(1):100-4
Authors: Meissner A, Sørensen OW
The conventional HNCA pulse sequence suffers from the ambiguity that it cannot distinguish inter- and intraresidue correlations because the one-bond and two-bond J(NC(alpha)) coupling constants are of similar magnitude. This paper presents a novel pulse sequence, sequential HNCA, that leads to a spectrum exhibiting...
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[NMR paper] NMR solution structure of the oxidized form of MerP, a mercuric ion binding protein i
NMR solution structure of the oxidized form of MerP, a mercuric ion binding protein involved in bacterial mercuric ion resistance.
Related Articles NMR solution structure of the oxidized form of MerP, a mercuric ion binding protein involved in bacterial mercuric ion resistance.
Biochemistry. 1998 Jun 30;37(26):9316-22
Authors: Qian H, Sahlman L, Eriksson PO, Hambraeus C, Edlund U, Sethson I
Mercuric ions are toxic to living organisms because of their strong affinity for cysteine residues in proteins. Some bacteria have developed a resistance...
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11-17-2010 11:06 PM
[NMR paper] NMR studies of the POU-specific DNA-binding domain of Oct-1: sequential 1H and 15N as
NMR studies of the POU-specific DNA-binding domain of Oct-1: sequential 1H and 15N assignments and secondary structure.
Related Articles NMR studies of the POU-specific DNA-binding domain of Oct-1: sequential 1H and 15N assignments and secondary structure.
Biochemistry. 1993 Jun 15;32(23):6032-40
Authors: Cox M, Dekker N, Boelens R, Verrijzer CP, van der Vliet PC, Kaptein R
The 1H and 15N resonances of the POU-specific DNA-binding domain of transcription factor Oct-1 have been assigned sequentially using two-dimensional homo- and heteronuclear...
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08-21-2010 11:53 PM
[NMR paper] Sequential assignment of the backbone nuclei (1H, 15N and 13C) of c-H-ras p21 (1-166)
Sequential assignment of the backbone nuclei (1H, 15N and 13C) of c-H-ras p21 (1-166).GDP using a novel 4D NMR strategy.
Related Articles Sequential assignment of the backbone nuclei (1H, 15N and 13C) of c-H-ras p21 (1-166).GDP using a novel 4D NMR strategy.
J Biomol NMR. 1992 Nov;2(6):639-46
Authors: Campbell-Burk SL, Domaille PJ, Starovasnik MA, Boucher W, Laue ED
The c-H-ras p21 protein is the product of the human ras proto-oncogene, a member of a ubiquitous eukaryotic gene family which is highly conserved in evolution. These proteins play...
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08-21-2010 11:45 PM
[NMR paper] 1H NMR studies of the glucocorticoid receptor DNA-binding domain: sequential assignme
1H NMR studies of the glucocorticoid receptor DNA-binding domain: sequential assignments and identification of secondary structure elements.
Related Articles 1H NMR studies of the glucocorticoid receptor DNA-binding domain: sequential assignments and identification of secondary structure elements.
Biochemistry. 1990 Sep 25;29(38):9015-23
Authors: HÀrd T, Kellenbach E, Boelens R, Kaptein R, Dahlman K, Carlstedt-Duke J, Freedman LP, Maler BA, Hyde EI, Gustafsson JA
Two protein fragments containing the DNA-binding domain (DBD) of the...
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Sequential Assignment of Spin systems
hi,
I am new to the protein NMR Field.I want to assign spin numbers to 120 amonoacid residues of a protein.I am cluless how to assing these number to each.Could anyone help me? Here is the primary sequence f a protein domain-
ISLLAQRQQF WIQLEFHSRI TRGERHGVID HVGLGVQSQQ RSNGFLTSLC ILRPHYASLS LALEKAQLHS LLCEETDGEG TLEYGFMGQV KSRFTDLSRP NLFCRHLGQL LPLLRVCRDV
I am expecing your help.Thank you.
ppaudyal
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03-13-2009 03:14 PM
Sequential Assignment of a proteing sequence
hi,
I am new to the protein NMR Field.I want to assign spin numbers to 120 amonoacid residues of a protein.I am cluless how to assign these number to each.Could anyone help me? Here is the primary sequence of a protein domain-
ISLLAQRQQF WIQLEFHSRI TRGERHGVID HVGLGVQSQQ RSNGFLTSLC ILRPHYASLS LALEKAQLHS LLCEETDGEG TLEYGFMGQV KSRFTDLSRP NLFCRHLGQL LPLLRVCRDV
I am expecing your help.Could any one do it on some software program and send to me in my email pkp08@yahoo.com.Thank you.
1H NMR studies of the mercuric ion binding protein MerP: sequential assignment, secon
Linear Mode
