Conformational Dependence of Electronic Coupling Across Peptide Bonds: A Ramachandran Map

2010 ◽  
Vol 114 (48) ◽  
pp. 20809-20812 ◽  
Author(s):  
Joseph B. Issa ◽  
Karsten Krogh-Jespersen ◽  
Stephan S. Isied
Keyword(s):  
Electronic Coupling ◽  
Peptide Bonds ◽  
Ramachandran Map

Peptide models XXIX. cis – trans Isomerism of peptide bonds: ab initio study on small peptide model compound; the 3D-Ramachandran map of formylglycinamide

2000 ◽  
Vol 500 (1-3) ◽  
pp. 97-111 ◽  
Author(s):  
H.A. Baldoni ◽  
G.N. Zamarbide ◽  
R.D. Enriz ◽  
E.A. Jauregui ◽  
Ö. Farkas ◽  
...  
Keyword(s):  
Ab Initio ◽  
Model Compound ◽  
Ab Initio Study ◽  
Small Peptide ◽  
Peptide Bonds ◽  
Ramachandran Map ◽  
Peptide Models

Studies on the Degradation of Human Fibrinogen by Plasmin and Trypsin

1966 ◽  
Vol 16 (03/04) ◽  
pp. 526-540 ◽  
Author(s):  
E. A Beck ◽  
D. P Jackson
Keyword(s):  
Physicochemical Properties ◽  
Electrophoretic Mobility ◽  
Rapid Loss ◽  
Clotting System ◽  
Human Fibrinogen ◽  
Peptide Bonds ◽  
Physico Chemical ◽  
Starch Gel ◽  
Ph Stat ◽  
Rapid Appearance

SummaryThe effects of trypsin and plasmin on the functional and physicochemical properties of purified human fibrinogen were observed at various stages of proteolysis. Concentrations of plasmin and trypsin that produced fibrinogenolysis at comparable rates as measured in a pH stat produced, at similar rates, loss of precipitability of fibrinogen by heat and ammonium sulphate and alterations in electrophoretic mobility on starch gel. Trypsin produced a more rapid loss of clottability of fibrinogen and a more rapid appearance of inhibitors of the thrombin-fibrinogen clotting system than did plasmin. Consistent differences were noted between the effects of trypsin and plasmin on the immunoelectrophoretic properties of fibrinogen during the early stages of proteolysis.These results are consistent with the hypothesis that trypsin initially reacts with the same peptide bonds of fibrinogen that are split by thrombin, but these same bonds do not appear to be split initially by plasmin. Measurement of the various functional and physico-chemical changes produced by the action of trypsin and plasmin on fibrinogen can be used to recognize various stages of proteolysis.

Stereodivergent Alkyne Hydrofluorination Using a Simple Practical Reagent

2020 ◽  
Author(s):  
Rui Guo ◽  
Xiaotian Qi ◽  
Hengye Xiang ◽  
Paul Geaneoates ◽  
Ruihan Wang ◽  
...  
Keyword(s):  
Bond Formation ◽  
Biologically Active ◽  
Dft Studies ◽  
Thermodynamic Control ◽  
Important Goal ◽  
Peptide Bonds ◽  
Metal Free ◽  
Vinyl Cation ◽  
E And Z Isomers ◽  
Vinyl Fluorides

Vinyl fluorides play an important role in drug development as they serve as bioisosteres for peptide bonds and are found in a range of biologically active molecules. The discovery of safe, general and practical procedures to prepare vinyl fluorides remains an important goal and challenge for synthetic chemistry. Here we introduce an inexpensive and easily-handled reagent and report simple, scalable, and metal-free protocols for the regioselective and stereodivergent hydrofluorination of alkynes to access both the E and Z isomers of vinyl fluorides. These conditions were suitable for a diverse collection of alkynes, including several highly-functionalized pharmaceutical derivatives. Mechanistic and DFT studies support C–F bond formation through a vinyl cation intermediate, with the (E)- and (Z)-hydrofluorination products forming under kinetic and thermodynamic control, respectively.<br>

scholarly journals Thermochromic aggregation-induced dual phosphorescence via temperature-dependent sp3-linked donor-acceptor electronic coupling

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Tao Wang ◽  
Zhubin Hu ◽  
Xiancheng Nie ◽  
Linkun Huang ◽  
Miao Hui ◽  
...  
Keyword(s):  
Excited State ◽  
Room Temperature ◽  
Electronic Coupling ◽  
Temperature Dependent ◽  
Molecular Systems ◽  
Donor And Acceptor ◽  
Theoretical Investigations ◽  
Donor Acceptor ◽  
And Control ◽  
Two Temperature

AbstractAggregation-induced emission (AIE) has proven to be a viable strategy to achieve highly efficient room temperature phosphorescence (RTP) in bulk by restricting molecular motions. Here, we show that by utilizing triphenylamine (TPA) as an electronic donor that connects to an acceptor via an sp3 linker, six TPA-based AIE-active RTP luminophores were obtained. Distinct dual phosphorescence bands emitting from largely localized donor and acceptor triplet emitting states could be recorded at lowered temperatures; at room temperature, only a merged RTP band is present. Theoretical investigations reveal that the two temperature-dependent phosphorescence bands both originate from local/global minima from the lowest triplet excited state (T1). The reported molecular construct serves as an intermediary case between a fully conjugated donor-acceptor system and a donor/acceptor binary mix, which may provide important clues on the design and control of high-freedom molecular systems with complex excited-state dynamics.

scholarly journals THE DETERMINATION OF PEPTIDE BONDS IN CRYSTALLINE LACTOGLOBULIN

1939 ◽  
Vol 131 (1) ◽  
pp. 387-395
Author(s):  
Rollin D. Hotchkiss
Keyword(s):  
Peptide Bonds

scholarly journals Nonenzymatic Cleavage of Peptide Bonds: The Methionine Residues in Bovine Pancreatic Ribonuclease

1962 ◽  
Vol 237 (6) ◽  
pp. 1856-1860 ◽  
Author(s):  
Erhard Gross ◽  
Bernhard Witkop
Keyword(s):  
Peptide Bonds ◽  
Pancreatic Ribonuclease ◽  
Methionine Residues

scholarly journals Cleavage of tryptophanyl peptide bonds in cytochrome b5 by cyanogen bromide.

1977 ◽  
Vol 252 (17) ◽  
pp. 5986-5989 ◽  
Author(s):  
J Ozols ◽  
C Gerard
Keyword(s):  
Cyanogen Bromide ◽  
Cytochrome B5 ◽  
Peptide Bonds

Permanent Dipole Moments Enhance Electronic Coupling and Singlet Fission in Pentacene

2021 ◽  
pp. 7453-7458
Author(s):  
Clemens Zeiser ◽  
Luca Moretti ◽  
Thomas Geiger ◽  
Lukas Kalix ◽  
Ana M. Valencia ◽  
...  
Keyword(s):  
Dipole Moments ◽  
Electronic Coupling ◽  
Singlet Fission
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