Results 41 to 50 of about 1,647 (123)
Secondary and Tertiary Structure of Bacteriorhodopsin in the SDS Denatured State
We characterized the structure of partially unfolded bacteriorhodopsin in sodium dodecyl sulfate (SDS) micelles and compared it with its in vitro refolded structure after reconstitution with dimyristoylphosphatidylcholine/3-[(3-cholamidopropyl ...
Balachandra G. Hegde (2113699) +3 more
core +1 more source
UV photoexcitation of adjacent intra‐strand pyrimidines in DNA can promote their covalent dimerization at sites such as 5′‐T‐p‐T‐3′ and 5′‐T‐p‐C‐3′. This photo‐reactivity leads, notably, to cyclobutane pyrimidine dimers, pyrimidine (6‐4) pyrimidone photoproducts (6‐4PPs), and, in bacterial endospores, the spore photoproduct, SP.
Ritu Chaturvedi, Eric C. Long
wiley +1 more source
MutM is a bacterial DNA glycosylase that serves as the first line of defense against the highly mutagenic 8-oxoguanine (oxoG) lesion, catalyzing glycosidic bond cleavage of oxoG to initiate base excision DNA repair.
Verdine, Gregory L. +3 more
core +1 more source
Ion pairing interactions between oppositely charged amino acids are important for protein structure stability. Despite the apparent electrostatic nature of these interactions, the charged amino acids Lys, Arg, Glu, and Asp have a different number of ...
Wang, Wei-Ren +3 more
core +2 more sources
Oligonucleotide‐Based Photoaffinity Probes: Chemical Tools and Applications for Protein Labeling
Photoactivatable oligonucleotides in combination with recent developments in mass spectrometry are powerful tools for studying nucleic acid‐protein interactions involved in numerous biological processes. In this review, we provide a comprehensive overview of the different strategies for incorporating the most used photoreactive reagents into ...
Carole Saintomé +3 more
wiley +1 more source
Pharmacological chaperones (PC's) are an emerging class of cell permeant small molecules that can stabilise the folding of misfolded variant proteins, thus restoring function. G protein‐coupled receptors (GPCRs) are a family of plasma membrane associated receptors that have been shown to be amenable to PC rescue.
Tarryn Radomsky +3 more
wiley +1 more source
Effect of Glutamate Side Chain Length on Intrahelical Glutamate–Lysine Ion Pairing Interactions
Ion pairing interactions between oppositely charged amino acids are important for protein structure stability. Despite the apparent electrostatic nature of these interactions, the charged amino acids Lys, Arg, Glu, and Asp have a different number of ...
Prashant Girinath (2046004) +10 more
core +1 more source
On the basis of revealing the ternary interaction mechanism of multiple biomacromolecules (amylose [AM], lauric acid [LA], and β‐lactoglobulin [βLG]) through experiments and simulation calculations, a thermally controlled hierarchical strategy was firstly reported for self‐assembly of AM–LA–βLG complex into uniform‐sized nanospheres with well‐defined ...
Chen Chao +6 more
wiley +1 more source
Activation mechanisms and structural dynamics of STIM proteins
Abstract Figure STIM activation involves a series of conformational rearrangements that transform the protein from a quiescent, tight state (left) into an active, extended state (right). While the exact series of events is still unresolved, currently available structural resolutions of STIM represent key pieces in solving the puzzle of STIM activation.
Matthias Sallinger +6 more
wiley +1 more source
A set of orthogonal, de novo coiled coil peptides are established comprising 3.5 heptads in length and a single buried Asn to prescribe dimer formation. The designed sequences display excellent partner fidelity. Interhelical E@g‐N@a interactions coordinate an extensive 6‐residue hydrogen bonding network that keeps the interchain Asn‐Asn′ contact in ...
Anthony R. Perez +3 more
wiley +1 more source

