Results 121 to 130 of about 114,428 (345)

Lack of self-averaging in neutral evolution of proteins

, 2002
We simulate neutral evolution of proteins imposing conservation of the thermodynamic stability of the native state in the framework of an effective model of folding thermodynamics.
C. H. Langley, D. Graur, E. Bornberg-Bauer, E. Zuckerkandl, E. I. Shakhnovich, E. I. Shakhnovich, H. Eduardo Roman, J. McDonald, J.-L. King, J. H. Gillespie, J. H. Gillespie, J. U. Bowie, M. Kimura, Markus Porto, Michele Vendruscolo, N. Takahata, N. V. Dokholyan, P. Schuster, R. A. Goldstein, R. J. Britten, T. Ohta, T. Ohta, Ugo Bastolla, W. H. Li   +23 more
core   +1 more source

Femtosecond X-ray emission study of the spin cross-over dynamics in haem proteins

, 2020
In haemoglobin (consisting of four globular myoglobin-like subunits), the change from the low-spin (LS) hexacoordinated haem to the high spin (HS) pentacoordinated domed form upon ligand detachment and the reverse process upon ligand binding, represent ...
Bacellar, Camila, Bressler, Christian, Budarz, James, Cannelli, Oliviero, Chergui, Majed, Galler, Andreas, Gawelda, Wojciech, Higashimura, Chika, Ito, Hironori, Ito, Terumasa, Katayama, Tetsuo, Keane, Theo, Khakhulin, Dmitry, Kinschel, Dominik, Kudo, Shotaro, Kurahashi, Naoya, Lima, Frederico A., Mancini, Giulia F., Milne, Christopher J., Misawa, Kazuhiko, Nishitani, Junichi, Obara, Yuki, Penfold, Thomas, Rouxel, Jeremy R., Schulz, Sebastian, Sorokin, Boris, Suzuki, Toshinori, Yabashi, Makina, Zalden, Peter   +28 more
core   +1 more source

21 Tesla MRI Microimaging of Rat Heart by Superparamagnetic Antimyoglobin Bound Nanoparticles [PDF]

, 2008
Superparamagnetic iron-oxide bound antimyoglobin (SPIOM) characteristics were analyzed at different pH. After injecting SPIOM in heart, ex vivo magnetic resonance microimaging (MRM) technique was used to visualize microvasculature of rat heart including
Rakesh Sharma
core   +2 more sources

Copper(II) Inhibition of the SARS‐CoV‐2 Main Protease

Natural Sciences, Volume 5, Issue 3, July 2025.
Molecular Docking of Cu(II) Schiff‐Base Chelates to SARS‐CoV‐2 Mpro. Two distinct Cu(II) chelates (Cu(II)Lp and Cu(II)Lm) are shown docked within the active site pocket of the Mpro, interacting with key residues HIS 41 and CYS 145. ABSTRACT In an analysis of the structural stability of the coronavirus main protease (Mpro), we identified regions of the ...
Roberto A. Garza‐López, Liam Kwak, Andrew Chung, Gabriel L. Ancajas, John J. Kozak, Harry B. Gray   +5 more
wiley   +1 more source

Quantum Criticality at the Origin of Life [PDF]

, 2015
Why life persists at the edge of chaos is a question at the very heart of evolution. Here we show that molecules taking part in biochemical processes from small molecules to proteins are critical quantum mechanically.
Csabai, Istvan, Kaufmann, Stuart A., Nassimi, Ali, Salahub, Dennis, Vattay, Gabor   +4 more
core   +3 more sources

Enzyme‐Substrate Complex Formation and Electron Transfer in Nitrogenase‐Like Dark‐Operative Protochlorophyllide Oxidoreductase (DPOR)

ChemistryOpen, EarlyView.
Dark‐operative protochlorophyllide oxidoreductase (DPOR) participates in photosynthesis by catalyzing the ATP‐dependent reduction of protochlorophyllide to chlorophyllide. Structurally and mechanistically resembling nitrogenase, DPOR′s mechanism was investigated using visible spectroscopy.
Giada Bedendi, Plinio Maroni, Ross D. Milton   +2 more
wiley   +1 more source

Simple design of cast myoglobin/polyethyleneimine modified electrodes [PDF]

, 2006
Negatively charged myoglobin (at pH values above its isoelectric point) was immobilized with the positively charged polyion polyethyleneimine (PEI) on pyrolytic graphite electrodes.
Basséguy, Régine, Bergel, Alain, Pardo-Jacques, Aurélie   +2 more
core   +1 more source

Setting an Upper Limit on the Myoglobin Iron(IV)Hydroxide pKa: Insight into Axial Ligand Tuning in Heme Protein Catalysis

Journal of the American Chemical Society, 2014
To provide insight into the iron(IV)hydroxide pKa of histidine ligated heme proteins, we have probed the active site of myoglobin compound II over the pH range of 3.9–9.5, using EXAFS, Mössbauer, and resonance Raman spectroscopies.
Timothy H. Yosca, Rachel K. Behan, Courtney M. Krest, Elizabeth L Onderko, Matthew C Langston, Michael T. Green   +5 more
semanticscholar   +1 more source

Exploring the Hemoglobin T to R2 Path Using Gaussian Elastic Network Correlation Map Distance

Proteins: Structure, Function, and Bioinformatics, EarlyView.
ABSTRACT Proteins are dynamic and undergo conformational changes. These changes may affect the motions executed by different regions of the proteins and are reflected in the motion correlation map. A method to accurately measure these changes is presented and exemplified on a set of tetrameric Hemoglobin structures.
Yuval Valenci, Dror Tobi
wiley   +1 more source

Towards Quantitative Classification of Folded Proteins in Terms of Elementary Functions

, 2010
A comparative classification scheme provides a good basis for several approaches to understand proteins, including prediction of relations between their structure and biological function. But it remains a challenge to combine a classification scheme that
Andrei Krokhotin, Antti J. Niemi, O. M. Becker, Shuangwei Hu, Xubiao Peng   +4 more
core   +1 more source