Results 351 to 360 of about 1,312,330 (378)

THE GENETICS OF DISULFIDE BOND METABOLISM

Annual Review of Genetics, 1998
▪ Abstract  Disulfide bonds are required for the stability and function of a large number of proteins. Genetic analysis in combination with biochemical studies have elucidated the main catalysts involved in facilitating these processes in the cell. All enzymes involved in thiol-disulfide metabolism have a conserved active site that consists of two ...
Arne Rietsch, Jonathan Beckwith
openaire   +2 more sources

Cytoglobin ligand binding regulated by changing haem-co-ordination in response to intramolecular disulfide bond formation and lipid interaction.

Biochemical Journal, 2015
Cytoglobin (Cygb) is a hexa-co-ordinate haem protein from the globin superfamily with a physiological function that is unclear. We have previously reported that the haem co-ordination is changed in the presence of lipids, potentially transforming the ...
Penny Beckerson, Michael T. Wilson, D. Svistunenko, B. Reeder   +3 more
semanticscholar   +1 more source

The position of disulfide bonds in cobrotoxin

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1970
Abstract 1. 1. The positions of four disulfide bonds in cobrotoxin were investigated. Cobrotoxin was digested with acid protease A, and the resulting five cystine peptides were separated by high-voltage electrophoresis on paper. The identification of the disulfide bridges was made by determining the amino acid composition of the corresponding ...
R.H.C. Chiu, H.J. Yang, C.C. Yang
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Thiol–Disulfide Exchange in Signaling: Disulfide Bonds As a Switch

Antioxidants & Redox Signaling, 2013
The major function of disulfide bonds is not only the stabilization of protein structures. Over the last 30 years, a change in perspective took place driven by groundbreaking experiments, which promoted disulfide bonds to central players in essential thiol-disulfide exchange reactions involved in signal transduction, thiol protection, and redox ...
Messens, Joris, Collet, Jean François
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Sequential Formation of Regioselective Disulfide Bonds in Synthetic Peptides with Multiple Disulfide Bonds

ChemInform, 2013
AbstractReview: 15 refs.
Mohammed Akhter Hossain, John D. Wade, Feng Lin, Fazel Shabanpoor   +3 more
openaire   +4 more sources

Stabilization of the cysteine-rich conotoxin MrIA by using a 1,2,3-triazole as a disulfide bond mimetic.

Angewandte Chemie, 2015
The design of disulfide bond mimetics is an important strategy for optimising cysteine-rich peptides in drug development. Mimetics of the drug lead conotoxin MrIA, in which one disulfide bond is selectively replaced of by a 1,4-disubstituted-1,2,3 ...
A. Gori, Ching-I A. Wang, P. Harvey, K. Rosengren, Rebecca F. Bhola, M. Gelmi, R. Longhi, M. Christie, Richard J. Lewis, P. Alewood, A. Brust   +10 more
semanticscholar   +1 more source

Disulfide-bond scrambling promotes amorphous aggregates in lysozyme and bovine serum albumin.

Journal of Physical Chemistry B, 2015
Disulfide bonds are naturally formed in more than 50% of amyloidogenic proteins, but the exact role of disulfide bonds in protein aggregation is still not well-understood.
Mu Yang, Colina Dutta, A. Tiwari
semanticscholar   +1 more source

Disulfide Bond in Diethyl Disulfide: A Rotational Spectroscopic Study

The Journal of Physical Chemistry A, 2018
Diethyl disulfide was investigated by pulsed jet Fourier transform microwave spectroscopy. The spectroscopic study was complemented by ab initio calculations. The first two most stable conformers predicted at the MP2/6-311++G(d,p) level of theory were observed in the supersonic expansion. Two 13C and one 34S isotopologues for the most stable conformer (
Jiaqi Zhang, Xiaolong Li, Qian Gou, Gang Feng   +3 more
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How Proteins Form Disulfide Bonds

Antioxidants & Redox Signaling, 2011
The identification of protein disulfide isomerase, almost 50 years ago, opened the way to the study of oxidative protein folding. Oxidative protein folding refers to the composite process by which a protein recovers both its native structure and its native disulfide bonds.
Joris Messens, Joris Messens, Jean-François Collet, Matthieu Depuydt   +3 more
openaire   +4 more sources

Disulfide Bonding in Protein Biophysics

Annual Review of Biophysics, 2012
It has been known for many decades that cell surface, soluble-secreted, and extracellular matrix proteins are generally rich in disulfide bonds, but only more recently has the functional diversity of disulfide bonding in extracellular proteins been appreciated.
openaire   +3 more sources