Zobrazeno 1 - 10
of 115
pro vyhledávání: '"Junji, Iwahara"'
Autor:
Binhan Yu, Junji Iwahara
Publikováno v:
Computational and Structural Biotechnology Journal, Vol 19, Iss , Pp 2279-2285 (2021)
Ionic interactions are crucial to biological functions of DNA, RNA, and proteins. Experimental research on how ions behave around biological macromolecules has lagged behind corresponding theoretical and computational research. In the 21st century, q
Externí odkaz:
https://doaj.org/article/5dd73fd8813b4c42b92efc892df448ae
Publikováno v:
Methods. 210:1-9
Nuclear magnetic resonance (NMR) spectroscopy is a versatile tool used to investigate the dynamic properties of biological macromolecules and their complexes. NMR relaxation data can provide order parameters S
Publikováno v:
The Journal of Physical Chemistry Letters. 13:10025-10029
Electrostatic potentials around macromolecules in the presence of mobile charges are difficult to assess especially for highly charged systems. Here, we report measurements of local electrostatic potentials around DNA by paramagnetic NMR. Through qua
Publikováno v:
Biophysical Journal. 121:3562-3570
Counterions are important constituents for the structure and function of nucleic acids. Using
Autor:
Binhan Yu, Junji Iwahara
Publikováno v:
Biopolymers.
Publikováno v:
Biochemistry. 61:1415-1418
Publikováno v:
J Phys Chem B
Experimental validation of theoretical models for protein electrostatics remains rare. Recently, we have developed a paramagnetic NMR-based method for de novo determination of effective near-surface electrostatic potentials, which allows for straight
Publikováno v:
Nucleic Acids Research.
In eukaryotes, many DNA/RNA-binding proteins possess intrinsically disordered regions (IDRs) with large negative charge, some of which involve a consecutive sequence of aspartate (D) or glutamate (E) residues. We refer to them as D/E repeats. The fun
Publikováno v:
Analytical Chemistry. 94:2444-2452
Publikováno v:
J Phys Chem Lett
Hindered rotation about a sp(2) C-N bond is known to occur in arginine (Arg), asparagine (Asn), and glutamine (Gln) side chains of proteins. However, very little is known about the rotational dynamics of Asn and Gln side-chain NH(2) groups. Here, usi