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biochemistry & molecular biology (50) 50
animals (37) 37
alpha-chymotrypsin (34) 34
protein conformation (27) 27
models, molecular (25) 25
cattle (24) 24
kinetics (24) 24
pancreatic trypsin-inhibitor (22) 22
molecular sequence data (20) 20
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trypsin (16) 16
index medicus (14) 14
resolution (14) 14
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serine endopeptidases - chemistry (10) 10
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serine proteinase inhibitors - chemistry (9) 9
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strong ligand-binding (9) 9
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analysis (8) 8
aprotinin - metabolism (8) 8
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bovine pancreatic α-chymotrypsin (8) 8
complex (8) 8
crystallography, x-ray (8) 8
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bovine pancreatic alpha-chymotrypsin (7) 7
chemistry, physical (7) 7
peptides (7) 7
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enzyme activation (6) 6
hydrogen bonding (6) 6
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acetonitrile (4) 4
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Chemical Physics Letters, ISSN 0009-2614, 12/2017, Volume 689, pp. 156 - 161
Journal Article
Thermochimica Acta, ISSN 0040-6031, 2002, Volume 382, Issue 1, pp. 151 - 160
Calorimetric heat effects and integral absorbance changes observed in the FTIR spectra were measured at immersing solid bovine pancreatic α-chymotrypsin in... 
Bovine pancreatic α-chymotrypsin | Organic solvent | FTIR-spectroscopy | Interactions enthalpies | Isothermal immersion calorimetry | interactions enthalpies | MIXTURES | CHEMISTRY, ANALYTICAL | bovine pancreatic alpha-chymotrypsin | HUMAN SERUM-ALBUMIN | CHEMISTRY, PHYSICAL | MEDIA | isothermal immersion calorimetry | organic solvent | WATER
Journal Article
Thermochimica Acta, ISSN 0040-6031, 2005, Volume 426, Issue 1, pp. 1 - 6
Journal Article
Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Enzymology, ISSN 0167-4838, 2001, Volume 1547, Issue 2, pp. 359 - 369
Journal Article
Journal Article
JOURNAL OF MOLECULAR BIOLOGY, ISSN 0022-2836, 05/1999, Volume 289, Issue 1, pp. 175 - 186
Different families of protein inhibitors of serine proteases share similar conformation of the enzyme-binding loop, while their scaffoldings are completely... 
EGLIN-C | COMPLEX | KUNITZ-TYPE DOMAIN | VI COLLAGEN | BETA-TRYPSIN | ACTIVE-SITE | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | additivity | PROTEIN-PROTEIN RECOGNITION | bovine pancreatic trypsin inhibitor | ALPHA-CHYMOTRYPSIN | trypsin | HUMAN-LEUKOCYTE | leukocyte elastase | chymotrypsin
Journal Article
International Journal of Biological Macromolecules, ISSN 0141-8130, 06/2019, Volume 131, pp. 473 - 483
In this study, the impact of spermidine on the stability, conformation and activity of elastase was investigated at the pH of 8.5 (the optimum pH for elastase)... 
Protein stability | Elastase | Kinetics | Spermidine | Quenching | THERMAL-STABILITY | POLYMER SCIENCE | ENZYME-ACTIVITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRYPSIN | LYSOZYME | OXIDE NANOPARTICLES | POLYAMINES | ALPHA-CHYMOTRYPSIN | BINDING-AFFINITY | CHEMISTRY, APPLIED | BOVINE SERUM-ALBUMIN | AGGREGATION | Enzymes | Hydrogen
Journal Article
Journal of Molecular Liquids, ISSN 0167-7322, 09/2019, Volume 289, p. 111115
The growing use of enzymes in various industries has created the need to study their interactions with different ligands. In this study, structural changes and... 
Protein stability | Elastase | Putrescine | Quenching | Circular dichroism | THERMAL-STABILITY | ENZYME-ACTIVITY | PHYSICS, ATOMIC, MOLECULAR & CHEMICAL | CHEMISTRY, PHYSICAL | CIRCULAR-DICHROISM SPECTRA | TRYPTOPHAN FLUORESCENCE | NANOPARTICLES | POLYAMINES | ALPHA-CHYMOTRYPSIN | PROTEINS | BINDING | BOVINE SERUM-ALBUMIN
Journal Article
Protein Science, ISSN 0961-8368, 12/2004, Volume 13, Issue 12, pp. 3139 - 3150
α‐Chymotrypsin undergoes a reversible conformational change from an inactive chymotrypsinogen‐like structure at high pH to an active conformation at neutral... 
letter “r,” rat variants | rΔAac, active conformation of rat chymotrypsin without propeptide | ΔA‐chymotrypsin, variants without propeptide (A‐chain) | A‐chain (propeptide) | bΔAin, inactive conformation of bovine chymotrypsin without propeptide | molecular dynamics simulation | conformational change | TMD, targeted molecular dynamics | letter “b,” bovine variants | MD, molecular dynamics | ac, active form | targeted molecular dynamics | pathway calculation | chymotrypsinogen | in, inactive form | bWTac, active conformation of bovine wild‐type chymotrypsin | rms, root mean square | rmsd, root mean square deviation | WT, wild‐type variants with pro‐peptide (A‐chain) | rΔAin, inactive conformation of rat chymotrypsin without propeptide | bΔAac, active conformation of bovine chymotrypsin without propeptide | bWTin, inactive conformation of bovine wild‐type chymotrypsin | chymotrypsin | fluorescence stopped flow | Targeted molecular dynamics | Chymotrypsin | Fluorescence stopped flow | Pathway calculation | Molecular dynamics simulation | A-chain (propeptide) | Chymotrypsinogen | Conformational change | PROTEIN | TARGETED MOLECULAR-DYNAMICS | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | BOVINE TRYPSINOGEN | REFINEMENT | PRESSURE | REFOLDING TRANSITION | PANCREATIC TRYPSIN-INHIBITOR | STRONG LIGAND-BINDING | Amino Acid Sequence | Signal Transduction | Chymotrypsin - metabolism | Enzyme Precursors - physiology | Models, Molecular | Molecular Sequence Data | Rats | Sequence Alignment | Animals | Time Factors | Cattle | Computer Simulation | Protein Conformation | Enzyme Activation | Hydrogen-Ion Concentration
Journal Article