Cancer-related mutations in BRCA1-BRCT cause long-range structural changes in protein-protein binding sites: A molecular dynamics study

2006 ◽  
Vol 66 (1) ◽  
pp. 69-86 ◽  
Author(s):  
Craig A. Gough ◽  
Takashi Gojobori ◽  
Tadashi Imanishi
Keyword(s):  
Molecular Dynamics ◽  
Protein Binding ◽  
Long Range ◽  
Binding Sites ◽  
Structural Changes ◽  
Protein Binding Sites

Searching for protein binding sites from Molecular Dynamics simulations and paramagnetic fragment-based NMR studies

2014 ◽  
Vol 1844 (3) ◽  
pp. 561-566 ◽  
Author(s):  
Andrea Bernini ◽  
Lucia Henrici De Angelis ◽  
Edoardo Morandi ◽  
Ottavia Spiga ◽  
Annalisa Santucci ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Protein Binding ◽  
Molecular Dynamics Simulations ◽  
Binding Sites ◽  
Nmr Studies ◽  
Protein Binding Sites ◽  
Dynamics Simulations

scholarly journals Differential BUM-HMM: a robust statistical modelling approach for detecting RNA flexibility changes in high-throughput structure probing data

2020 ◽  
Author(s):  
Paolo Marangio ◽  
Ka Ying Toby Law ◽  
Guido Sanguinetti ◽  
Sander Granneman
Keyword(s):  
Protein Binding ◽  
High Throughput ◽  
Conformational Changes ◽  
Binding Sites ◽  
Rna Structure ◽  
Structural Changes ◽  
High Throughput Sequencing ◽  
Structural Information ◽  
Protein Binding Sites ◽  
Structure Probing

Combining RNA structure probing with high-throughput sequencing technologies has greatly enhanced our ability to analyze RNA structure at transcriptome scale. However, the high level of noise and variability encountered in these data call for the development of computational tools that robustly extract RNA structural information. Here we present diffBUM-HMM, a noise-aware model that enables accurate detection of RNA flexibility and conformational changes from high-throughput RNA structure-probing data. DiffBUM-HMM is compatible with a wide variety of high-throughput RNA structure probing data, taking into consideration biological variation, sequence coverage and sequence representation biases. We demonstrate that, compared to the existing approaches, diffBUM-HMM displays higher sensitivity while calling virtually no false positives. DiffBUM-HMM analysis of ex vivo and in vivo Xist SHAPE-MaP data detected many more RNA structural differences, involving mostly single-stranded nucleotides located at or near protein-binding sites. Collectively, our analyses demonstrate the value of diffBUM-HMM for quantitatively detecting RNA structural changes and reinforce the notion that RNA structure probing is a very powerful tool for identifying protein-binding sites.

Long-Range Distance Measurements of Protein Binding Sites by Rotational-Echo Double-Resonance NMR

1996 ◽  
Vol 118 (23) ◽  
pp. 5476-5477 ◽  
Author(s):  
Daniel R. Studelska ◽  
Christopher A. Klug ◽  
Denise D. Beusen ◽  
Lynda M. McDowell ◽  
Jacob Schaefer
Keyword(s):  
Protein Binding ◽  
Long Range ◽  
Binding Sites ◽  
Double Resonance ◽  
Distance Measurements ◽  
Protein Binding Sites ◽  
Rotational Echo Double Resonance

EVALUATION OF TISSUE STEROID BINDING IN VITRO

1971 ◽  
Vol 68 (1_Suppl) ◽  
pp. S223-S246 ◽  
Author(s):  
C. R. Wira ◽  
H. Rochefort ◽  
E. E. Baulieu
Keyword(s):  
Protein Binding ◽  
Binding Sites ◽  
Experimental System ◽  
Specific Protein ◽  
Coupling Mechanism ◽  
Target Tissue ◽  
Protein Binding Sites ◽  
Definition Of ◽  
Hormone Specificity

ABSTRACT The definition of a RECEPTOR* in terms of a receptive site, an executive site and a coupling mechanism, is followed by a general consideration of four binding criteria, which include hormone specificity, tissue specificity, high affinity and saturation, essential for distinguishing between specific and nonspecific binding. Experimental approaches are proposed for choosing an experimental system (either organized or soluble) and detecting the presence of protein binding sites. Techniques are then presented for evaluating the specific protein binding sites (receptors) in terms of the four criteria. This is followed by a brief consideration of how receptors may be located in cells and characterized when extracted. Finally various examples of oestrogen, androgen, progestagen, glucocorticoid and mineralocorticoid binding to their respective target tissues are presented, to illustrate how researchers have identified specific corticoid and mineralocorticoid binding in their respective target tissue receptors.

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