about
Structure determination of a small protein through a 23-dimensional molecular-replacement searchStructure of HrcQB-C, a conserved component of the bacterial type III secretion systemsStructure determination through homology modelling and torsion-angle simulated annealing: application to a polysaccharide deacetylase from Bacillus cereusCharacterizing a partially ordered miniprotein through folding molecular dynamics simulations: Comparison with the experimental data.Loopless Rop: structure and dynamics of an engineered homotetrameric variant of the repressor of primer protein.Order through disorder: hyper-mobile C-terminal residues stabilize the folded state of a helical peptide. a molecular dynamics studyProtein flexibility and enzymatic catalysis.Three force fields' views of the 3(10) helix.Reconstruction of DNA sequences using genetic algorithms and cellular automata: towards mutation prediction?The 11th misconception?On the application of Good-Turing statistics to quantify convergence of biomolecular simulations.Ionic strength reducers: an efficient approach to protein purification and crystallization. Application to two Rop variants.Grcarma: A fully automated task-oriented interface for the analysis of molecular dynamics trajectories.Using J-coupling constants for force field validation: application to hepta-alanine.Determination of protein oligomerization state: two approaches based on glutaraldehyde crosslinking.As good as it gets? Folding molecular dynamics simulations of the LytA choline-binding peptide result to an exceptionally accurate model of the peptide structure.Folding Simulations of a Nuclear Receptor Box-Containing Peptide Demonstrate the Structural Persistence of the LxxLL Motif Even in the Absence of Its Cognate Receptor.Unusual α-Carbon Hydroxylation of Proline Promotes Active-Site Maturation.Pinda: a web service for detection and analysis of intraspecies gene duplication events.On the foldability of tryptophan-containing tetra- and pentapeptides: an exhaustive molecular dynamics study.Sensitivity of Folding Molecular Dynamics Simulations to Even Minor Force Field Changes.Multidimensional molecular replacement.On the distribution of the bulk-solvent correction parameters.A stochastic approach to molecular replacement.Low-resolution structural characterization of the arginine repressor/activator from Bacillus subtilis: a combined X-ray crystallographic and electron microscopical approach.Crystallization of type I chloramphenicol acetyltransferase: an approach based on the concept of ionic strength reducers.A fast and inexpensive procedure for drying polyacrylamide gelsCrystallization and diffraction to ultrahigh resolution (0.8 A) of a designed variant of the Rop proteinMeaningful refinement of polyalanine models using rigid-body simulated annealing: application to the structure determination of the A31P Rop mutantSoftware news and updates. Carma: a molecular dynamics analysis programMolecular Dynamics Simulations of BcZBP, A Deacetylase from Bacillus cereus: Active Site Loops Determine Substrate Accessibility and SpecificityFolding molecular dynamics simulations accurately predict the effect of mutations on the stability and structure of a vammin-derived peptideMolecular simulation of peptides coming of age: Accurate prediction of folding, dynamics and structuresOn the presence of short-range periodicities in protein structures that are not related to established secondary structure elements
P50
Q27640819-C92D9562-DD53-4E2E-A8B2-740B2BC54734Q27642850-5C1E92FA-E756-4DB8-8A46-5E45E81931A4Q27683952-1DD30970-08F4-4B4E-B342-5104B144F00DQ31028368-3E6C7FC5-6508-41EC-A919-3F8DE3E505B2Q33343121-54DB8252-661B-4779-BD77-0F45867977AFQ33781118-C1A3ADC7-8547-4BBA-A9F8-335AC31EC832Q38011286-1F895B92-4892-4713-B52E-5A69C78BBE4FQ38597579-AD4D046F-7677-4DEB-AF47-3C6EA8F2C378Q40127850-4DFE1F5D-728F-4CAA-89C8-28195BE25F12Q42147682-27592654-6603-4195-B5AE-002E390C8F48Q42634364-983F90E9-AE87-4A71-A2FD-90FB019F3588Q44949170-DC46D853-80DB-4875-94E5-E2FCE62895C5Q45909863-3321C29F-DE3F-4E7C-BBA2-78D7230F521CQ46021245-72ED4CD9-A386-427E-A834-84781C9D1C8AQ46893147-FBC03C64-DA56-4811-8254-B832DFCBCF9CQ46984821-CF119FD6-3106-44B6-90BA-0C7BB361D87BQ47766529-1C94F575-7DBF-41E9-ABBF-4504CCDE7150Q48370198-00101D05-31BC-413F-9544-865A9A997EB0Q50882593-8E1BF619-BB8E-4924-BE01-FDF88C78C8EAQ51062330-BB64FA2D-E4D7-411F-8102-7D03C6558069Q51453077-15608E6E-BBF4-44FD-B52F-BF05761DDCDBQ52054864-0E719B26-9CD4-4807-9600-549924AFC479Q52075248-C0ABDB98-4437-437A-9675-5F2BE2069261Q52082103-A36ACE56-4FD6-4E26-A5BC-92994E7BCFA2Q52866680-0EBC3E36-9B4B-401A-ACD2-74EB0602758EQ54063253-29AB6AA1-571C-4A15-9196-73775E7A8DDFQ73190697-026F0D22-CDD7-4CA0-B1E0-D722D6201904Q74177283-427B949F-2761-47C0-9C09-FCA3A882F7ADQ77959491-34154DB9-7182-4B86-A26B-DA1551A9080EQ80135906-4E55CD27-E163-4BCF-A4DE-7397CF2F839FQ86790273-E646196D-BD95-4625-A6CA-FAECB9BDA432Q87513186-82EC5A2E-0E2D-4132-BF6A-A4E197201072Q91317305-D610347A-0D4F-440A-BBFD-BE220B14C77DQ92737932-884519D7-4E14-43E2-B92F-CAB5EA968449
P50
description
hulumtues
@sq
researcher
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wetenschapper
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հետազոտող
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name
Nicholas M. Glykos
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Nicholas M. Glykos
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Nicholas M. Glykos
@es
Nicholas M. Glykos
@nl
Nicholas M. Glykos
@sl
type
label
Nicholas M. Glykos
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Nicholas M. Glykos
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Nicholas M. Glykos
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Nicholas M. Glykos
@nl
Nicholas M. Glykos
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prefLabel
Nicholas M. Glykos
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Nicholas M. Glykos
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Nicholas M. Glykos
@es
Nicholas M. Glykos
@nl
Nicholas M. Glykos
@sl
P106
P1153
6603617104
P21
P2456
P31
P496
0000-0003-3782-206X