1H- and31P-nmr studies of ditercalinium binding to a d(GCGC)2 and d(CCTATAGG)2 minihelices: A sequence specificity study

Biopolymers ◽  
1991 ◽  
Vol 31 (3) ◽  
pp. 331-353 ◽  
Author(s):  
Muriel Delepierre ◽  
Catherine Milhe ◽  
Abdelkader Namane ◽  
Tam Huynh Dinh ◽  
Bernard P. Roques
Keyword(s):  
Sequence Specificity ◽  
Nmr Studies ◽  
Specificity Study

scholarly journals Two distinct binding modes provide the RNA binding protein RbFox with extraordinary sequence specificity

2021 ◽  
Author(s):  
Xuan Ye ◽  
Wen Yang ◽  
Soon Yi ◽  
Yanan Zhao ◽  
Fan Yang ◽  
...  
Keyword(s):  
Binding Site ◽  
Protein Interactions ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Rna Recognition Motif ◽  
Rna Recognition ◽  
Sequence Specificity ◽  
Binding Modes ◽  
Nmr Studies ◽  
Second Mode

The specificity of RNA-binding proteins for their target sequences varies considerably. Yet, it is not understood how certain proteins achieve markedly higher sequence specificity than most others. Here we show that the RNA Recognition Motif of RbFox accomplishes extraordinary sequence specificity by employing functionally and structurally distinct binding modes. Affinity measurements of RbFox for all binding site variants reveal the existence of two different binding modes. The first exclusively binds the cognate and a closely related RNA variant with high affinity. The second mode accommodates all other RNAs with greatly reduced affinity, thereby imposing large thermodynamic penalties on even near-cognate sequences. NMR studies indicate marked structural differences between the two binding modes, including large conformational rearrangements distant from the RNA binding site. Distinct binding modes by a single RNA binding module explain extraordinary sequence selectivity and reveal an unknown layer of functional diversity, cross talk and regulation for RNA-protein interactions.

Antitumour drug–DNA interactions: NMR studies of echinomycin and chromomycin complexes

1989 ◽  
Vol 22 (2) ◽  
pp. 93-138 ◽  
Author(s):  
Xiaolian Gao ◽  
Dinshaw J. Patel
Keyword(s):  
Intelligent Design ◽  
Hydrogen Exchange ◽  
Recent Progress ◽  
Molecular Level ◽  
Drug Binding ◽  
Sequence Specificity ◽  
Dna Interactions ◽  
Nmr Studies ◽  
Antitumour Agents ◽  
Antitumour Drug

The intelligent design of new families of DNA-binding antitumour agents must await an understanding at the molecular level of the structure, dynamics and energetics of drug-DNA interactions on currently available systems. Recent progress in this area has been significant and reflects the interplay between footprinting methods that identify the sequence specificity of drug binding, structural approaches that define conformational features in the crystalline and solution states, hydrogen exchange techniques that monitor transient base pair opening and calorimetric methods that partition the enthalpic and entropic contributions to the binding isotherm.

NMR studies of the R2 repeat and related peptide fragments of the DNA binding domain of c-Myb. New light on the structure and folding of R2.

1999 ◽  
Vol 96 (9/10) ◽  
pp. 1580-1584 ◽  
Author(s):  
I. Ségalas ◽  
S. Desjardins ◽  
H. Oulyadi ◽  
Y. Prigent ◽  
S. Tribouillard ◽  
...  
Keyword(s):  
Dna Binding ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Peptide Fragments ◽  
Nmr Studies ◽  
Related Peptide

2D NMR studies on muscle and cerebral metabolism in vivo

1994 ◽  
Vol 91 ◽  
pp. 697-703 ◽  
Author(s):  
B Gillet ◽  
BT Doan ◽  
C Verre-Sebrie ◽  
O Fedeli ◽  
JC Beloeil ◽  
...  
Keyword(s):  
Cerebral Metabolism ◽  
2D Nmr ◽  
Nmr Studies

NMR STUDIES OF CONCENTRATED LITHIUM-AMMONIA SOLUTIONS

1980 ◽  
Vol 41 (C8) ◽  
pp. C8-32-C8-35
Author(s):  
Y. Nakamura ◽  
M. Niibe ◽  
M. Shimoji
Keyword(s):  
Nmr Studies

NMR STUDIES OF Co-BASED NITRIDE AMORPHOUS FILMS

1988 ◽  
Vol 49 (C8) ◽  
pp. C8-1713-C8-1714
Author(s):  
K. Le Dang ◽  
P. Veillet ◽  
H. Sakakima ◽  
R. Krishnan
Keyword(s):  
Amorphous Films ◽  
Nmr Studies

Physico-Chemical Properties of Recombinant Desulphatohirudin

1990 ◽  
Vol 63 (03) ◽  
pp. 499-504 ◽  
Author(s):  
A Electricwala ◽  
L Irons ◽  
R Wait ◽  
R J G Carr ◽  
R J Ling ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Gel Filtration ◽  
Chemical Properties ◽  
Alpha Helix ◽  
Apparent Molecular Weight ◽  
Correlation Spectroscopy ◽  
Nmr Studies ◽  
Recombinant Hirudin ◽  
Physico Chemical ◽  
Recombinant Molecule

SummaryPhysico-chemical properties of recombinant desulphatohirudin expressed in yeast (CIBA GEIGY code No. CGP 39393) were reinvestigated. As previously reported for natural hirudin, the recombinant molecule exhibited abnormal behaviour by gel filtration with an apparent molecular weight greater than that based on the primary structure. However, molecular weight estimation by SDS gel electrophoresis, FAB-mass spectrometry and Photon Correlation Spectroscopy were in agreement with the theoretical molecular weight, with little suggestion of dimer or aggregate formation. Circular dichroism studies of the recombinant molecule show similar spectra at different pH values but are markedly different from that reported by Konno et al. (13) for a natural hirudin-variant. Our CD studies indicate the presence of about 60% beta sheet and the absence of alpha helix in the secondary structure of recombinant hirudin, in agreement with the conformation determined by NMR studies (17)

Sign in / Sign up

Export Citation Format

Share Document