scispace - formally typeset
Journal ArticleDOI

Determination of the helix and beta form of proteins in aqueous solution by circular dichroism.

Yee-Hsiung Chen, +2 more
- 30 Jul 1974 - 
- Vol. 13, Iss: 16, pp 3350-3359
About
This article is published in Biochemistry.The article was published on 1974-07-30. It has received 1986 citations till now. The article focuses on the topics: Circular dichroism & Helix.

read more

Citations
More filters
Journal ArticleDOI

pH-dependent pore formation properties of pardaxin analogues.

TL;DR: The interaction of pardaxin, a shark-repellent neurotoxin, and its charge-modified analogues with vesicles and human erythrocytes is described and a direct correlation between alpha-helical content, the analogues' hydrophobicity, and their pore-forming properties at the different pH values tested is shown.
Journal ArticleDOI

Conformation and stability of the anion transport protein of human erythrocyte membranes.

TL;DR: Circular dichroism studies of membranes that had been digested extensively with proteolytic enzymes and stripped of all extrinsic fragments revealed that the portions of red cell membrane proteins that are embedded in the lipid bilayer contain a very high content of alpha-helix.
Journal ArticleDOI

Solution structure of the 45-residue MgATP-binding peptide of adenylate kinase as examined by 2-D NMR, FTIR, and CD spectroscopy.

TL;DR: The structure of a synthetic peptide corresponding to residues 1-45 of rabbit muscle adenylate kinase has been studied in aqueous solution by two-dimensional NMR, FTIR, and CD spectroscopy, suggesting that the resolution-enhanced amide I band of the peptide FTIR spectrum is broad and rather featureless, possibly due to disorder, it can be fit by using methods developed on well-characterized globular proteins.
Journal ArticleDOI

The native ensemble and folding of a protein molten-globule: functional consequence of downhill folding.

TL;DR: The simulations reveal a connection between downhill folding and large conformational flexibility in this domain that has been evolutionarily selected and functionally exploited resulting in large binding promiscuity and suggests that the thermodynamic features of molten-globules fall within the array of folding mechanisms available to small single-domain proteins.
Journal ArticleDOI

Deuterium exchange of α‐helices and β‐sheets as monitored by electrospray ionization mass spectrometry

TL;DR: Deuterium exchange was monitored by electrospray ionization mass spectrometry (ESI‐MS) to study the slowly exchanging (hydrogen bonded) peptide hydrogens of several α‐helical peptides and β‐sheet proteins.
References