Search Results - "Garbuzynskiy, Sergiy O"
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FoldAmyloid: a method of prediction of amyloidogenic regions from protein sequence
Published in Bioinformatics (01-02-2010)“…Motivation: Amyloidogenic regions in polypeptide chains are very important because such regions are responsible for amyloid formation and aggregation. It is…”
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Prediction of amyloidogenic and disordered regions in protein chains
Published in PLoS computational biology (01-12-2006)“…The determination of factors that influence protein conformational changes is very important for the identification of potentially amyloidogenic and disordered…”
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Golden triangle for folding rates of globular proteins
Published in Proceedings of the National Academy of Sciences - PNAS (02-01-2013)“…The ability of protein chains to spontaneously form their spatial structures is a long-standing puzzle in molecular biology. Experimentally measured rates of…”
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Correction: Finkelstein et al. How Can Ice Emerge at 0 °C? Biomolecules 2022, 12 , 981
Published in Biomolecules (Basel, Switzerland) (23-11-2023)“…We regret to state that our article "How Can Ice Emerge at 0 °C?" [...]…”
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Calculation of Crystal-Solution Dissociation Constants
Published in Biomolecules (Basel, Switzerland) (18-01-2022)“…The calculation of dissociation constants is an important problem in molecular biophysics. For such a calculation, it is important to correctly calculate both…”
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FoldUnfold: web server for the prediction of disordered regions in protein chain
Published in Bioinformatics (01-12-2006)“…Identification of disordered regions in polypeptide chains is very important because such regions are essential for protein function. A new parameter, namely…”
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How Can Ice Emerge at 0 °C?
Published in Biomolecules (Basel, Switzerland) (13-07-2022)“…The classical nucleation theory shows that bulk water freezing does not occur at temperatures above ≈ -30 °C, and that at higher temperatures ice nucleation…”
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Intrinsic disorder in protein interactions: insights from a comprehensive structural analysis
Published in PLoS computational biology (01-03-2009)“…We perform a large-scale study of intrinsically disordered regions in proteins and protein complexes using a non-redundant set of hundreds of different protein…”
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Physics of Ice Nucleation and Antinucleation: Action of Ice-Binding Proteins
Published in Biomolecules (Basel, Switzerland) (01-01-2024)“…Ice-binding proteins are crucial for the adaptation of various organisms to low temperatures. Some of these, called antifreeze proteins, are usually thought to…”
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Contact order revisited: Influence of protein size on the folding rate
Published in Protein science (01-09-2003)“…Guided by the recent success of empirical model predicting the folding rates of small two‐state folding proteins from the relative contact order (CO) of their…”
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Different packing of external residues can explain differences in the thermostability of proteins from thermophilic and mesophilic organisms
Published in Bioinformatics (01-09-2007)“…Motivation: Understanding the basis of protein stability in thermophilic organisms raises a general question: what structural properties of proteins are…”
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Protein folding problem: enigma, paradox, solution
Published in Biophysical reviews (01-12-2022)“… The ability of protein chains to spontaneously form their three-dimensional structures is a long-standing mystery in molecular biology. The most conceptual…”
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Backbone Carbonyl Group Basicities Are Related to Gas-Phase Fragmentation of Peptides and Protein Folding
Published in Angewandte Chemie International Edition (01-01-2007)“…A strong correlation is found between the propensity of individual amino acids to induce peptide‐bond cleavage in the gas phase (PAA–XX) and their…”
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Sublimation Entropy and Dissociation Constants Prediction by Quantitative Evaluation of Molecular Mobility in Crystals
Published in The journal of physical chemistry letters (06-07-2017)“…Prediction of binding free energies (or dissociation constants) is a crucial challenge for computational biochemistry. One of the main problems here consists…”
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Reduction of the Search Space for the Folding of Proteins at the Level of Formation and Assembly of Secondary Structures: A New View on the Solution of Levinthal's Paradox
Published in Chemphyschem (16-11-2015)“…The complete volume of the protein conformation space is, by many orders of magnitude, smaller at the level of secondary structure elements than that at the…”
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Clarification to “Protein folding problem: enigma, paradox, solution”
Published in Biophysical reviews (01-04-2023)Get full text
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Restrictions to protein folding determined by the protein size
Published in FEBS letters (27-06-2013)“…Experimentally measured rates of spontaneous folding of single-domain globular proteins range from microseconds to hours: the difference (11 orders of…”
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There and back again: Two views on the protein folding puzzle
Published in Physics of life reviews (01-07-2017)“…The ability of protein chains to spontaneously form their spatial structures is a long-standing puzzle in molecular biology. Experimentally measured folding…”
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Levinthal's question answered ... again?
Published in Journal of biomolecular structure & dynamics (01-09-2013)Get full text
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