X
Search Filters
Format Format
Format Format
X
Sort by Item Count (A-Z)
Filter by Count
Journal Article (2492) 2492
Publication (174) 174
Book Chapter (16) 16
Book Review (5) 5
Newspaper Article (4) 4
Conference Proceeding (3) 3
Paper (1) 1
more...
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
thermolysin (1603) 1603
biochemistry & molecular biology (938) 938
amino acid sequence (918) 918
animals (682) 682
thermolysin - metabolism (519) 519
molecular sequence data (476) 476
kinetics (435) 435
binding sites (433) 433
humans (414) 414
trypsin (384) 384
protein conformation (369) 369
thermolysin - chemistry (345) 345
models, molecular (331) 331
amino acids - analysis (298) 298
proteins (298) 298
hydrolysis (291) 291
index medicus (283) 283
peptide fragments - analysis (264) 264
protein binding (244) 244
chymotrypsin (231) 231
biophysics (221) 221
binding (205) 205
enzymes (200) 200
hydrogen-ion concentration (191) 191
chromatography, gel (188) 188
catalysis (180) 180
cattle (179) 179
substrate specificity (179) 179
molecular weight (175) 175
chemistry (173) 173
structure-activity relationship (160) 160
peptides (156) 156
biotechnology & applied microbiology (155) 155
cyanogen bromide (150) 150
electrophoresis, polyacrylamide gel (145) 145
thermolysin - antagonists & inhibitors (143) 143
temperature (141) 141
thermodynamics (135) 135
chromatography, high pressure liquid (129) 129
ligands (126) 126
purification (125) 125
research (125) 125
peptides - analysis (122) 122
inhibitors (121) 121
analysis (116) 116
chromatography, ion exchange (116) 116
metalloendopeptidases - chemistry (116) 116
crystallography, x-ray (113) 113
circular dichroism (112) 112
proteases (111) 111
mutagenesis, site-directed (110) 110
molecular structure (109) 109
chemistry, multidisciplinary (108) 108
stability (108) 108
metalloendopeptidases - metabolism (107) 107
protein structure, tertiary (107) 107
protease (106) 106
protein folding (106) 106
peptide fragments - chemistry (103) 103
rats (103) 103
protein denaturation (102) 102
chemistry, medicinal (101) 101
carboxypeptidases (100) 100
crystal-structure (99) 99
enzyme stability (98) 98
resolution (98) 98
proteolysis (94) 94
escherichia-coli (92) 92
expression (91) 91
food science & technology (91) 91
protein structure, secondary (90) 90
trypsin - metabolism (90) 90
electrophoresis, paper (89) 89
zinc (89) 89
peptide fragments - metabolism (88) 88
protein (88) 88
bacillus - enzymology (86) 86
drug design (86) 86
peptide fragments - isolation & purification (85) 85
mechanism (84) 84
peptides - isolation & purification (83) 83
chemistry, organic (82) 82
endopeptidases - metabolism (82) 82
chemical phenomena (81) 81
research article (81) 81
mass spectrometry (79) 79
recombinant proteins - chemistry (79) 79
cell biology (78) 78
macromolecular substances (78) 78
peptides - chemistry (78) 78
enzyme (76) 76
hot temperature (76) 76
recombinant proteins - metabolism (76) 76
thermolysin - pharmacology (76) 76
base sequence (75) 75
zinc - metabolism (75) 75
hydrogen bonding (74) 74
mice (74) 74
species specificity (73) 73
active-site (72) 72
more...
Language Language
Publication Date Publication Date
Click on a bar to filter by decade
Slide to change publication date range


Acta Crystallographica Section D, ISSN 1399-0047, 11/2015, Volume 71, Issue 11, pp. 2328 - 2343
Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 02/2006, Volume 128, Issue 4, pp. 1070 - 1071
Journal Article
Journal Article
PLoS ONE, ISSN 1932-6203, 10/2012, Volume 7, Issue 10, p. e46147
The biophysical stability is an important parameter for protein activity both in vivo and in vitro. Here we propose a method to analyse thermal melting of... 
GREEN FLUORESCENT PROTEIN | IN-VITRO | PYRUVATE-KINASE | THERMOLYSIN | NMR-SPECTROSCOPY | SCANNING CALORIMETRY | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | P53 CORE DOMAIN | ALPHA-SYNUCLEIN | BINDING PROTEIN | Cysteine Endopeptidases - chemistry | Temperature | Heme - metabolism | Protein Unfolding | Aminoacyltransferases - genetics | Bacterial Proteins - chemistry | Thermolysin - metabolism | Chemistry Techniques, Analytical - methods | Maltose - chemistry | Cytochromes c - chemistry | Cysteine Endopeptidases - metabolism | Heme - chemistry | Proteolysis | Maltose-Binding Proteins - chemistry | Protein Denaturation | Protein Stability | Protein Structure, Tertiary | Aminoacyltransferases - chemistry | Maltose - metabolism | Reproducibility of Results | Biophysical Phenomena | Cytochromes c - metabolism | Electrophoresis, Polyacrylamide Gel | Bacterial Proteins - genetics | Maltose-Binding Proteins - metabolism | Protein Folding | Proteins - genetics | Point Mutation | Proteins - metabolism | Cysteine Endopeptidases - genetics | Protein Binding | Aminoacyltransferases - metabolism | Bacterial Proteins - metabolism | Kinetics | Proteins - chemistry | Proteins | Fluorescence | Protein engineering | Automation | Cooling | Stability | Temperature gradients | Biochemistry | Laboratory equipment | Kinases | Gene expression | Temperature gradient | Lysates | Biomedical materials | Reaction time | Ligands | In vivo methods and tests | Mutation | Methods | Cancer
Journal Article
Peptides, ISSN 0196-9781, 2011, Volume 32, Issue 2, pp. 388 - 400
▶ Identification of peptides. ▶ LC–MS and protein databases. ▶ Novel antioxidants. Sarcoplasmic proteins isolated from bovine livers were hydrolyzed using the... 
Bovine by-products | Sacroplasmic proteins | Antioxidant peptides | Thermolysin | FRAP | DPPH radical scavenging activity assay | Fe 2+ chelating ability assay | chelating ability assay | Fe | LIPID OXIDATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | IONIZATION-MASS SPECTROMETRY | MUSCLE | FRAME PROTEIN | IDENTIFICATION | ENZYME-INHIBITORY PEPTIDES | MEAT | Fe2+ chelating ability assay | CONSECUTIVE CHROMATOGRAPHY | GELATIN HYDROLYSATE | PHARMACOLOGY & PHARMACY | SKIN | Antioxidants - chemistry | Free Radical Scavengers - chemistry | Water - analysis | Pulmonary Surfactant-Associated Protein A - analysis | Ferric Compounds - chemistry | Thermolysin - metabolism | Proteins - analysis | Chlorides - chemistry | Chromatography, High Pressure Liquid | Fatty Acid-Binding Proteins - metabolism | snRNP Core Proteins - metabolism | Liver Extracts - metabolism | Iron Chelating Agents - chemistry | alpha-Globins - analysis | Spectrometry, Mass, Electrospray Ionization | Cattle | Picrates - chemistry | Ferrous Compounds - chemistry | Biphenyl Compounds - chemistry | Antioxidants - analysis | Large-Conductance Calcium-Activated Potassium Channel alpha Subunits - analysis | Cytoplasm - chemistry | Amino Acid Sequence | Filtration | Protein Hydrolysates - chemistry | Peptides - chemistry | Nitrogen - analysis | Liver Extracts - chemistry | Large-Conductance Calcium-Activated Potassium Channel alpha Subunits - metabolism | Pulmonary Surfactant-Associated Protein A - metabolism | Catalase - metabolism | Animals | Proteins - metabolism | beta-Globins - metabolism | Fatty Acid-Binding Proteins - analysis | beta-Globins - analysis | Catalase - analysis | snRNP Core Proteins - analysis | Proteins - chemistry | Peptides - analysis | Protein Hydrolysates - analysis | alpha-Globins - metabolism | Proteins | Antioxidants | Polyvinylidene fluoride | Iron compounds | Safety and security measures | Questions and answers | Amino acids | Chemical properties | Glutamate | Mass spectrometry | Food | Enzymes | Microorganisms | Peptides | Liver | Byproducts | Assaying
Journal Article
Journal Article
Chemical Science, ISSN 2041-6520, 2018, Volume 9, Issue 15, pp. 3710 - 3715
Protein glycosylation is a diverse post-translational modification that serves myriad biological functions. O-linked glycans in particular vary widely in... 
MANNOSYLATION | BACTERIA | AFFINITY | TRICHODERMA-REESEI | REGIONS | RESISTANCE | GLYCOSYLATION | PROTEOLYSIS | CHEMISTRY, MULTIDISCIPLINARY | LINKER | CELLULASE | Proteins | Eukaryotes | Yeast | Stability | Computer simulation | Molecular dynamics | Thermolysin | Mannose | Stiffening | Galactose | Glycan | Hydroxyl groups | synthesis | 09 BIOMASS FUELS | glycans | proteolysis protection | intrinsically disordered proteins
Journal Article
Chemical Communications, ISSN 1359-7345, 01/2015, Volume 51, Issue 8, pp. 1520 - 1523
Journal Article
Journal of Computer-Aided Molecular Design, ISSN 0920-654X, 9/2006, Volume 20, Issue 9, pp. 567 - 587
Journal Article
Critical Reviews in Food Science and Nutrition, ISSN 1040-8398, 01/2017, Volume 57, Issue 2, pp. 418 - 453
Proteins in solution are subject to myriad forces stemming from interactions with each other as well as with the solvent media. The role of the environmental... 
Acid Protease A | Whey proteins | selective hydrolysis | α-lactalbumin | pH-stat | β-lactoglobulin | BOVINE BETA-LACTOGLOBULIN | FILTER MEMBRANE REACTOR | ENZYME-INHIBITORY-ACTIVITY | HIGH-HYDROSTATIC-PRESSURE | FOOD SCIENCE & TECHNOLOGY | MULTIVARIATE DATA-ANALYSIS | RESPONSE-SURFACE METHODOLOGY | NATIVE ALPHA-LACTALBUMIN | alpha-lactalbumin | beta-lactoglobulin | PERFORMANCE LIQUID-CHROMATOGRAPHY | NUTRITION & DIETETICS | HEAT-INDUCED DENATURATION/AGGREGATION | MAILLARD REACTION-PRODUCTS | Enzymes, Immobilized - metabolism | Protein Hydrolysates - metabolism | Temperature | Chymotrypsin - metabolism | Thermolysin - metabolism | Food Additives - chemistry | Pepsin A - chemistry | Protein Hydrolysates - isolation & purification | Whey Proteins - metabolism | Osmolar Concentration | Proteolysis | Protein Denaturation | Food Handling | Buffers | Enzymes, Immobilized - chemistry | Peptide Fragments - metabolism | Biocatalysis | Food Additives - isolation & purification | Protein Hydrolysates - chemistry | Peptide Fragments - isolation & purification | Thermolysin - chemistry | Solubility | Pepsin A - metabolism | Trypsin - metabolism | Whey Proteins - chemistry | Peptide Fragments - chemistry | Animals | Whey Proteins - isolation & purification | Chymotrypsin - chemistry | Food Additives - metabolism | Protein Conformation | Trypsin - chemistry | Hydrogen-Ion Concentration | Proteins | Enzymes | Food science | Molecular structure
Journal Article