about
Sublimation Entropy and Dissociation Constants Prediction by Quantitative Evaluation of Molecular Mobility in Crystals.Threading with chemostructural restrictions method for predicting fold and functionally significant residues: application to dipeptidylpeptidase IV (DPP-IV).Average and extreme multi-atom Van der Waals interactions: strong coupling of multi-atom Van der Waals interactions with covalent bonding.Perfect temperature for protein structure prediction and folding.Protein structure: what is it possible to predict now?Residue-residue mean-force potentials for protein structure recognition.What is the probability of a chance prediction of a protein structure with an rmsd of 6 A?Optimization of protein structure on lattices using a self-consistent field approach.Golden triangle for folding rates of globular proteins.There and back again: Two views on the protein folding puzzle.A structural perspective of compensatory evolutionMaking optimal use of empirical energy functions: force-field parameterization in crystal space.Alpha-helix and beta-hairpin Folding from experiment, analytical theory and molecular dynamics simulations.Prediction of protein folding rates from the amino acid sequence-predicted secondary structure.Restrictions to protein folding determined by the protein size.Recognition of signal sequences.Contact order revisited: influence of protein size on the folding rate.How to determine the size of folding nuclei of protofibrils from the concentration dependence of the rate and lag-time of aggregation. I. Modeling the amyloid protofibril formation.Search for the stable state of a short chain in a molecular field.Levinthal's question answered … again?Theory of protein molecule self-organization. III. A calculating method for the probabilities of the secondary structure formation in an unfolded polypeptide chain.Did the primitive ribosomal RNA code primitive ribosomal protein?Structural model for interferons.Adjusting potential energy functions for lattice models of chain molecules.How to determine the size of folding nuclei of protofibrils from the concentration dependence of the rate and lag-time of aggregation. II. Experimental application for insulin and LysPro insulin: aggregation morphology, kinetics, and sizes of nucleiCunning simplicity of a stoichiometry driven protein folding thesis.What is Responsible for Atypical Dependence of the Rate of Amyloid Formation on Protein Concentration: Fibril-Catalyzed Initiation of New Fibrils or Competition with Oligomers?Development and testing of PFFSol1.1, a new polarizable atomic force field for calculation of molecular interactions in implicit water environment.Search for the most stable folds of protein chains: II. Computation of stable architectures of beta-proteins using a self-consistent molecular field theory.Computation of biopolymers: a general approach to different problems.Protein folding as flow across a network of folding-unfolding pathways. 2. The "in-water" case.Protein folding as flow across a network of folding-unfolding pathways. 1. The mid-transition case.Many-atom van der Waals interactions lead to direction-sensitive interactions of covalent bonds.From analysis of protein structural alignments toward a novel approach to align protein sequences.Theoretical study of a landscape of protein folding-unfolding pathways. Folding rates at midtransition.Constructing lattice models of protein chains with side groups.A new approach to the design of a sequence with the highest affinity for a molecular surface.Theory of protein secondary structure and algorithm of its prediction.Time to overcome the high, long, and bumpy free energy barrier in a multi-stage process: the generalized steady-state approach.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.
P50
Q30101103-4782F05F-860E-40E2-B372-901814D6600DQ30330077-491146F3-FF23-4644-B688-282126FF4D15Q30364716-7079256F-C8CB-4784-8D3A-1B732C39C421Q30423608-7E7074E0-5BCB-4E97-829A-2CE62F75003EQ30426475-996AE5DF-7636-40CB-9CD3-A087563D58D5Q30429120-B0B89ECF-3EA7-46A6-A8FB-B58EBD9449D0Q30430314-625D395E-482D-4E55-A89C-6AAE15448AABQ30431671-6C500B4C-200A-4346-A4CE-02205F7F37ECQ33354907-5E7A5694-0376-46F6-A47E-18B538BA93B9Q33364756-F15F870F-83ED-498C-9B96-FDD49BBC38E3Q34079015-99DDBB12-3347-4008-AAA9-AE6EFA337D82Q34351595-79AAAF5C-B162-4343-9529-79B52E8D36A6Q34790633-9A9F38E7-273E-4CD6-9ADA-7C2D49D3D97DQ34830201-A1FFF948-663F-496C-99A1-4186CA900B75Q38107703-8596DB2B-49DB-42A2-B6A1-8CCBDBB57387Q41586987-2F12D2A4-EB95-4483-AC33-C172A117052EQ42115099-6A25EBF7-2801-4CC9-8B96-7BAC75692149Q42636713-7DBB706B-A218-4601-AFFE-F887C3E686B7Q43458590-E33EF56C-D2E3-4358-9C16-3A43B3D1A4E8Q43826979-C054CDA8-82BC-400C-827C-06F61F386A24Q44387063-29635D81-CA59-478F-9B9E-7BC9C63F37C2Q44697007-577F85B5-076E-41A4-BEBB-C8AB5A474E7CQ44994392-669CEDD0-B41D-45F2-977A-7CA07E390CD0Q46212567-9EC7293D-EEEF-4B10-8A86-9BCEFA81114DQ47188631-B64AB586-28AB-4F69-B054-BACCEA948C70Q48061243-FCB0A96B-3C03-45AD-A082-DB2912D4EB87Q50141145-FAC957BC-F6A8-4438-AA61-D74D7E0CBB41Q51603078-951BDBCB-C670-4039-B05D-0D9D8FD4A947Q51649644-532DD733-CD57-41CD-9332-7665697941D5Q51653521-21061B92-6A1B-46F8-AABF-03394F620D58Q51695397-D619CC2E-1FEE-44D6-989D-DEF3AE0B72AFQ51699926-0FB89EF2-A54B-480F-8E96-2F1877352CA7Q51870412-6D4A372A-98C1-4863-935C-AC83E31BB0A7Q52004497-82545FE0-94D3-488F-9B4E-0AFA3430ACC2Q52057125-A38D086D-3CF2-4198-BB21-2DB6333C1D5FQ52356049-2A5138F9-5631-4767-8DE3-7DF104BF2183Q52412439-5069BF9A-E402-475A-893E-C08825A256F8Q52710750-6EEDA1C6-487B-4AD9-A51E-09BF5865CB40Q53669860-FD8770F6-288C-4D35-BDBF-5FF2F6D37A1BQ53674504-C9D85553-B568-488B-AF99-B763C6F1571A