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Results 1 - 10
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612
The Effects of r-Helical Structure and Cyanylated Cysteine on Each Other
, 2010
"... -Thiocyanatoalanine, or cyanylated cysteine, is an artificial amino acid that can be introduced at solvent-exposed cysteine residues in proteins via chemical modification. Its facile post-translational synthesis means that it may find broad use in large protein systems as a probe of site-specific st ..."
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-repeat helix were synthesized containing cyanylated cysteine at different sites. The cyanylated cysteine side chain is shown to destabilize, but not completely disrupt, the helical structure of the folded peptide when substituted for alanine. In addition, the CtN stretching bandwidth of the artificial side
Short-Lived R-Helical Intermediates in the Folding of β-Sheet Proteins
, 2010
"... ABSTRACT: Several lines of evidence point strongly toward the importance of highly R-helical intermediates in the folding of all globular proteins, regardless of their native structure. However, experimental refolding studies demonstrate no observable R-helical intermediate during refolding of some ..."
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ABSTRACT: Several lines of evidence point strongly toward the importance of highly R-helical intermediates in the folding of all globular proteins, regardless of their native structure. However, experimental refolding studies demonstrate no observable R-helical intermediate during refolding of some
An R-Helical Burst in the src SH3 Folding Pathway
, 2006
"... ABSTRACT: Src SH3 is a small all-β-sheet protein composed of a single domain. We studied the folding behavior of src SH3 at various conditions by circular dichroism (CD), fluorescence, and X-ray solution scattering methods. On the src SH3 folding pathway, an R-helix-rich intermediate appeared not on ..."
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Cited by 1 (1 self)
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of the burst phase is proportional to the helical fraction calculated according to the helix-coil transition theory. This strongly suggests that the initial folding core is formed by the collapse of much less stably existing R-helices. The biological function of globular proteins is determined by their native
Uncoupled Peptide Bond Vibrations in r-Helical and Polyproline II Conformations of
, 2004
"... We examined the 204-nm UV resonance Raman (UVR) spectra of the polyproline II (PPII) and R-helical states of a 21-residue mainly alanine peptide (AP) in different H2O/D2O mixtures. Our hypothesis is that if the amide backbone vibrations are coupled, then partial deuteration of the amide N will pertu ..."
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Raman bands can be considered as being independently Raman scattered by the individual peptide bonds. This dramatically simplifies the use of these vibrational bands in IR and Raman studies of peptide and protein structure. In contrast, the AmI and AmI ′ bands of the R-helical conformation cannot
Molecular Dynamics Study of the Solvation of an r-Helical Transmembrane Peptide by DMSO
, 2007
"... A 10-ns molecular dynamics study of the solvation of a hydrophobic transmembrane helical peptide in dimethyl sulfoxide (DMSO) is presented. The objective is to analyze how this aprotic polar solvent is able to solvate three groups of amino acid residues (i.e., polar, apolar, and charged) that are lo ..."
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) that are located in a stable helical region of a transmembrane peptide. The 25-residue peptide (sMTM7) used mimics the cytoplasmic proton hemichannel domain of the seventh transmembrane segment (TM7) from subunit a of H+-V-ATPase from Saccharomyces cereVisiae. The three-dimensional structure of peptide sMTM7
A Stable Lipid-Induced Aggregate of r-Synuclein
"... R-Synuclein (RS) is a 140 residue protein constituting the major component of Lewy bodies found in Parkinson’s disease,1,2 where it is aggregated into fibrils.3 Although the exact function of RS is yet to be determined, the interaction of RS with synaptic vesicles has been suggested to be important ..."
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for its physiological role.3-5 While RS is natively unfolded in solution,6 upon binding to negatively charged membranes it adopts an amphipathic, R-helical structure involving residues 1-100.7-13 Membrane binding is also thought to affect fibrillization, although conflicting evidence exists on whether
Predicted Unfolding Order of the 13 r-Helices in the Catalytic Domain of Glucoamylase from Aspergillus awamori var. X100 by Molecular Dynamics Simulations
"... The unfolding mechanism of the 13 R-helices in the catalytic domain of Aspergillus awamori var. X100 glucoamylase was investigated by 200 ps molecular dynamics simulations in explicit water with temperature jump technique. Rather than a simultaneous event, the unfolding of these 13 R-helices followe ..."
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to unfold, indicating that the destruction of the secondary structure motif was initiated from the inner region of the catalytic domain. The dynamic behavior of these R-helices induced by increased kinetic energy during the unfolding process is considered to be similar to the expansion and compression of a
Coassembly of Synthetic Segments of Shaker K
"... : Increasing evidence suggests that membrane-embedded hydrophobic segments can interact within the phospholipid milieu of the membrane with varying degrees of specificity and thus contribute to the folding and oligomerization of proteins. We have used synthetic peptides corresponding to segments ..."
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with, and orientation within phospholipid membranes were examined. Secondary structure studies revealed that though S3 and S4 both adopt certain fractions of R-helical structures in membrane mimetic environments, the R-helical content of S3 is lower. Both S3 and S4 bind strongly to zwitterionic
The Effect of Aqueous Solvation upon r-Helix Formation for Polyalanines
"... The incremental free energies of aqueous solution for acetyl(ala) N NH 2 in its extended unfolded and R-helical conformations are compared using the SM5.2 solvation method of Cramer and Truhlar. A combination of density functional theory (DFT) at the B3LYP/D95(d,p) and AM1 has been employed using t ..."
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the ONIOM method. The incremental solvation energies of R-helical structures are very similar for both ONIOM and AM1 optimized structures as these structures do not significantly change upon solution. However, the conformations of the unfolded peptides change from extended -strand to polyproline II
Natively unfolded human prothymosin R adopts partially folded collapsed conformation at acidic pH
- Biochemistry
, 1999
"... ABSTRACT: Prothymosin R has previously been shown to be unfolded at neutral pH, thus belonging to a growing family of “natively unfolded ” proteins. The structural properties and conformational stability of recombinant human prothymosin R were characterized at neutral and acidic pH by gel filtration ..."
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Cited by 1 (0 self)
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state, with structural properties different from those of the molten globule. The formation of R-helical structure by the glutamic acid-rich elements of the protein accompanied by the partial hydrophobic collapse is expected at lower pH due to the neutralization of the negatively charged residues
Results 1 - 10
of
612
