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biochemistry & molecular biology (19) 19
molecular dynamics (17) 17
models, molecular (14) 14
humans (13) 13
protein-coupled receptors (12) 12
protein conformation (11) 11
index medicus (10) 10
receptors, oxytocin - chemistry (10) 10
receptors, vasopressin - chemistry (10) 10
rhodopsin (9) 9
biophysics (8) 8
computer simulation (8) 8
ligands (8) 8
computer science, interdisciplinary applications (7) 7
crystal-structure (7) 7
amino acid sequence (6) 6
arginine-vasopressin (6) 6
binding (6) 6
binding-site (6) 6
chemistry, multidisciplinary (6) 6
pharmacology & pharmacy (6) 6
proteins (6) 6
vasopressin (6) 6
activation (5) 5
alpha-subunit (5) 5
analysis (5) 5
animals (5) 5
automated docking (5) 5
chemistry (5) 5
protein binding (5) 5
simulated annealing (5) 5
vasopressins - chemistry (5) 5
amber (4) 4
antagonists (4) 4
chemistry, organic (4) 4
gpcr activation (4) 4
molecular docking (4) 4
molecular sequence data (4) 4
molecular-dynamics (4) 4
nephrogenic diabetes-insipidus (4) 4
particle mesh ewald (4) 4
peptides - chemistry (4) 4
phenylalanine - analogs & derivatives (4) 4
phenylalanine - chemistry (4) 4
phospholipid bilayer (4) 4
polypeptide-chains (4) 4
protein structure, tertiary (4) 4
receptor-ligand interactions (4) 4
simulation (4) 4
simulations (4) 4
united-residue model (4) 4
antagonist (3) 3
aromatic residues (3) 3
atosiban (3) 3
autodock (3) 3
avp (3) 3
backbone (3) 3
binding sites (3) 3
biochemical research methods (3) 3
cattle (3) 3
chemistry, analytical (3) 3
chemistry, medicinal (3) 3
crystallography (3) 3
dimerization (3) 3
drug discovery (3) 3
functional expression (3) 3
gpcr (3) 3
mathematical & computational biology (3) 3
model (3) 3
models (3) 3
models, chemical (3) 3
molecular-dynamics simulation (3) 3
neurohypophyseal hormone-receptors (3) 3
ot/vp receptors (3) 3
oxytocin - chemistry (3) 3
pharmacological-properties (3) 3
preterm labor (3) 3
proteins - chemistry (3) 3
receptors, oxytocin - metabolism (3) 3
receptors, vasopressin - metabolism (3) 3
residual dipolar couplings (3) 3
rhodopsin - chemistry (3) 3
sequence alignment (3) 3
stereoisomerism (3) 3
tests (3) 3
vancomycin (3) 3
5-hydroxytryptamine receptors (2) 2
acid side-chains (2) 2
alpha (2) 2
amino acid substitution (2) 2
amino acids - chemistry (2) 2
analytical formulas (2) 2
antidiuretic hormone receptor antagonists (2) 2
bioinformatics (2) 2
biophysical phenomena (2) 2
cell-wall (2) 2
cloning (2) 2
computer applications in chemistry (2) 2
conformation analysis (2) 2
conserved sequence (2) 2
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1. Full Text Performance of protein-structure predictions with the physics-based UNRES force field in CASP11
by Krupa, Paweł and Mozolewska, Magdalena A and Wiśniewska, Marta and Yin, Yanping and He, Yi and Sieradzan, Adam K and Ganzynkowicz, Robert and Lipska, Agnieszka G and Karczyńska, Agnieszka and Slusarz, Magdalena and Slusarz, Rafał and Giełdoń, Artur and Czaplewski, Cezary and Jagieła, Dawid and Zaborowski, Bartłomiej and Scheraga, Harold A and Liwo, Adam
Bioinformatics, ISSN 1367-4803, 11/2016, Volume 32, Issue 21, pp. 3270 - 3278
Participating as the Cornell-Gdansk group, we have used our physics-based coarsegrained UNited RESidue (UNRES) force field to predict protein structure in the... 
LOCAL CONFORMATIONAL STATES | POLYPEPTIDE-CHAINS | BIOCHEMICAL RESEARCH METHODS | MOLECULAR-DYNAMICS SIMULATION | MONTE-CARLO | ALL-ATOM | POTENTIAL-ENERGY FUNCTION | UNITED-RESIDUE MODEL | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | GLOBAL OPTIMIZATION | MATHEMATICAL & COMPUTATIONAL BIOLOGY | SYSTEMS | BACKBONE | Reproducibility of Results | Animals | Protein Structure, Secondary | Humans | Models, Molecular | Protein Conformation | Proteins - chemistry | Original Papers
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2. Full Text Lessons from application of the UNRES force field to predictions of structures of CASP10 targets
by Yi He and Magdalena A. Mozolewska and Paweł Krupa and Adam K. Sieradzan and Tomasz K. Wirecki and Adam Liwo and Khatuna Kachlishvili and Shalom Rackovsky and Dawid Jagieła and Rafał Ślusarz and Cezary R. Czaplewski and Stanisław Ołdziej and Harold A. Scheraga
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 9/2013, Volume 110, Issue 37, pp. 14936 - 14941
The performance of the physics-based protocol, whose main component is the United Residue (UNRES) physics-based coarse-grained force field, developed in our... 
Proteins | Simulations | Databases | Chirality | Force field | Molecular dynamics | Biochemistry | Topology | Modeling | Bioinformatics | Multi-domain packing | Structure symmetry | Protein folding | multi-domain packing | TESTS | MOLECULAR-DYNAMICS | POLYPEPTIDE-CHAINS | MEAN FORCE | MULTIDISCIPLINARY SCIENCES | ALPHA | ACID SIDE-CHAINS | REPLICA EXCHANGE | PROTEIN-STRUCTURE PREDICTION | structure symmetry | UNITED-RESIDUE MODEL | protein folding | ANALYTICAL FORMULAS | Biophysical Phenomena | Humans | Models, Molecular | Protein Conformation | Protein Interaction Domains and Motifs | Proteins - chemistry | Protein Folding | Research | Biophysics | Protein-protein interactions | Biological Sciences
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3. Full Text A unified coarse-grained model of biological macromolecules based on mean-field multipole–multipole interactions
by Liwo, Adam and Baranowski, Maciej and Czaplewski, Cezary and Gołaś, Ewa and He, Yi and Jagieła, Dawid and Krupa, Paweł and Maciejczyk, Maciej and Makowski, Mariusz and Mozolewska, Magdalena A and Niadzvedtski, Andrei and Ołdziej, Stanisław and Scheraga, Harold A and Sieradzan, Adam K and Ślusarz, Rafał and Wirecki, Tomasz and Yin, Yanping and Zaborowski, Bartłomiej
Journal of Molecular Modeling, ISSN 1610-2940, 8/2014, Volume 20, Issue 8, pp. 1 - 15
A unified coarse-grained model of three major classes of biological molecules—proteins, nucleic acids, and polysaccharides—has been developed. It is based on... 
Proteins | Theoretical and Computational Chemistry | Chemistry | Multipole–multipole interactions | Polysaccharides | Coarse-graining | Characterization and Evaluation of Materials | Molecular Medicine | Nucleic acids | Mean-field approach | Computer Applications in Chemistry | Computer Appl. in Life Sciences | Multipole-multipole interactions | MOLECULAR-DYNAMICS | POLYPEPTIDE-CHAINS | UNRES FORCE-FIELD | POTENTIAL-ENERGY LANDSCAPE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ACID SIDE-CHAINS | CHEMISTRY, MULTIDISCIPLINARY | PROTEIN-STRUCTURE PREDICTION | KNOWLEDGE-BASED POTENTIALS | COMPUTER SCIENCE, INTERDISCIPLINARY APPLICATIONS | BIOPHYSICS | UNITED-RESIDUE MODEL | MONTE-CARLO SIMULATIONS | ANALYTICAL FORMULAS | Macromolecular Substances - chemistry | Nucleic Acids - chemistry | Peptides - chemistry | Protein Structure, Secondary | Polysaccharides - chemistry | Protein Binding | Proteins - chemistry | Molecular Dynamics Simulation | Models | Analysis | Original Paper
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4. The oxolane ring opening of some muramic acid derivatives under acidic conditions
by Samaszko-Fiertek, Justyna and Dmochowska, Barbara and Ślusarz, Rafał and Madaj, Janusz
Letters in Organic Chemistry, ISSN 1570-1786, 2018, Volume 15, Issue 8, pp. 693 - 697
Synthesis of 1,6-anhydro sugars is well known in literature. The dioxolane ring exhibits at least two types of properties. It can be used as a protecting group... 
Ac | Dioxolane ring | 1,6-anhydro derivative | Sc(OTf) | TFA/Ac | Mur-derivative | Cleavage of 1,6-anhydro linkage | dioxolane ring | Sc(OTf)/Ac2O | CELL-WALL | PEPTIDOGLYCAN | cleavage of 1,6-anhydro linkage | ESCHERICHIA-COLI | TFA/Ac2O | CHEMISTRY, ORGANIC | H2SO4/ACO | LEVOGLUCOSAN
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5. Full Text Extension of the UNRES Coarse-Grained Force Field to Membrane Proteins in the Lipid Bilayer
by Zieba, K and Slusarz, M and Slusarz, R and Liwo, A and Czaplewski, C and Sieradzan, AK
JOURNAL OF PHYSICAL CHEMISTRY B, ISSN 1520-6106, 09/2019, Volume 123, Issue 37, pp. 7829 - 7839
The physics-based UNRES coarse-grained force field for the simulations of protein structure and dynamics has been extended to treat membrane proteins. The... 
TESTS | MOLECULAR-DYNAMICS | ENERGY | STRUCTURE SIMULATIONS | CHEMISTRY, PHYSICAL | COOPERATIVITY | MODEL | MARTINI | CHAINS | BACKBONE | STRUCTURE PREDICTION
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6. Full Text Interactions of vasopressin and oxytocin receptors with vasopressin analogues substituted in position 2 with 3,3′-diphenylalanine - a molecular docking study
: INTERACTIONS OF AVP ANALOGUES WITH RECEPTORS
by Ślusarz, Magdalena J and Sikorska, Emilia and Ślusarz, Rafał
Journal of Peptide Science, ISSN 1075-2617, 02/2013, Volume 19, Issue 2, pp. 118 - 126
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7. Full Text Molecular modeling of Gram-positive bacteria peptidoglycan layer, selected glycopeptide antibiotics and vancomycin derivatives modified with sugar moieties
by Ślusarz, Rafał and Szulc, Monika and Madaj, Janusz
Carbohydrate Research, ISSN 0008-6215, 05/2014, Volume 389, Issue 1, pp. 154 - 164
Proper understanding of the mechanisms of binding to Gram-positive bacteria cell wall layers—especially to the peptidoglycan (PG) layer, seems to be crucial... 
Conformation analysis | Peptidoglycan | Root mean square deviation | Molecular dynamic of sugar | Vancomycin derivatives | MUREIN PEPTIDOGLYCAN | CRYOELECTRON MICROSCOPY | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | CELL-WALL STRUCTURE | ENTEROCOCCUS-FAECALIS | PERIPLASMIC SPACE | CHEMISTRY, ORGANIC | TERTIARY STRUCTURE | BACILLUS-SUBTILIS 168 | FORCE-FIELD | STAPHYLOCOCCUS-AUREUS | CHEMISTRY, APPLIED | Peptidoglycan - metabolism | Amino Acid Sequence | Peptidoglycan - chemistry | Glycopeptides - chemistry | Aminoglycosides - chemistry | Anti-Bacterial Agents - metabolism | Vancomycin - metabolism | Molecular Dynamics Simulation | Glycopeptides - metabolism | Vancomycin - chemistry | Aminoglycosides - metabolism | Anti-Bacterial Agents - chemistry | Vancomycin - pharmacology | Anti-Bacterial Agents - pharmacology | Aminoglycosides - pharmacology | Carbohydrate Conformation | Glycopeptides - pharmacology | Staphylococcus aureus - drug effects | Bacillus subtilis - drug effects | Bacteria | Antibacterial agents | Models
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8. Full Text Influence of bulky 3,3′-diphenylalanine enantiomers replacing position 2 of AVP analogues on their conformations: NMR and molecular modeling studies
by Sikorska, Emilia and Kwiatkowska, Anna and Sobolewski, Dariusz and Ślusarz, Magdalena J and Ślusarz, Rafał
European Journal of Medicinal Chemistry, ISSN 0223-5234, 2010, Volume 45, Issue 9, pp. 4065 - 4073
In this paper we use NMR spectroscopy and molecular modeling to examine four vasopressin analogues substituted with bulky 3,3′-diphenylalanine (Dpa)... 
Arginine vasopressin analogues | V 2 agonists | Simulated annealing (SA) | 3,3-Diphenylalanine enantiomers | NMR spectroscopy | Antiuterotonic activity | agonists | SYSTEM | ELUCIDATION | CHEMISTRY, MEDICINAL | TEMPERATURE-DEPENDENCE | COUPLING-CONSTANTS | ARGININE-VASOPRESSIN | SPECTROSCOPY | V-2 agonists | DYNAMICS | BINDING | DESMOPRESSIN | OXYTOCIN RECEPTORS | Amino Acid Sequence | Arginine Vasopressin - analogs & derivatives | Phenylalanine - metabolism | Magnetic Resonance Spectroscopy | Phenylalanine - analogs & derivatives | Phenylalanine - chemistry | Stereoisomerism | Models, Molecular | Arginine Vasopressin - chemistry | Protein Conformation | Executives | Peptides | Heterocyclic compounds | Analysis | Nuclear magnetic resonance spectroscopy | Models | Enantiomers | Vasopressin
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9. Full Text Molecular Docking-Based Study of Vasopressin Analogues Modified at Positions 2 and 3 with N-Methylphenylalanine:  Influence on Receptor-Bound Conformations and Interactions with Vasopressin and Oxytocin Receptors
by Ślusarz, Magdalena J and Sikorska, Emilia and Ślusarz, Rafał and Ciarkowski, Jerzy
Journal of Medicinal Chemistry, ISSN 0022-2623, 04/2006, Volume 49, Issue 8, pp. 2463 - 2469
In this study, four cyclic vasopressin (CYFQNCPRG-NH2, AVP) analogues substituted at positions 2 and 3 with four combinations of enantiomers of... 
CHEMISTRY, MEDICINAL | DYNAMICS SIMULATION | CLONING | AUTOMATED DOCKING | RHODOPSIN | PROTEIN-COUPLED RECEPTORS | BINDING-SITE | 5-HYDROXYTRYPTAMINE(2A) RECEPTORS | AGONIST BINDING | NEUROHYPOPHYSEAL HORMONE-RECEPTORS | CONSERVED AROMATIC RESIDUES | Models, Chemical | Phenylalanine - analogs & derivatives | Stereoisomerism | Humans | Molecular Sequence Data | Structure-Activity Relationship | Vasopressins - chemistry | Receptors, Oxytocin - chemistry | Receptors, Vasopressin - chemistry | Cattle | Phenylalanine - chemistry | Computer Simulation | Imaging, Three-Dimensional | Binding Sites - drug effects | Protein Structure, Tertiary | Amino Acid Sequence | Magnetic Resonance Spectroscopy | Receptors, Oxytocin - antagonists & inhibitors | Models, Molecular | Vasopressins - pharmacology | Sequence Alignment | Animals | Ligands | Protein Conformation | Antidiuretic Hormone Receptor Antagonists | Amino Acid Substitution
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10. Full Text Interactions of vasopressin and oxytocin receptors with vasopressin analogues substituted in position 2 with 3,3′‐diphenylalanine – a molecular docking study
by Ślusarz, Magdalena J and Sikorska, Emilia and Ślusarz, Rafał
Journal of Peptide Science, ISSN 1075-2617, 02/2013, Volume 19, Issue 2, pp. 118 - 126
Vasopressin and oxytocin receptors belong to the superfamily of G protein‐coupled receptors and play an important role in many physiological functions. They... 
vasopressin analogues | vasopressin and oxytocin receptors | receptor–ligand interactions | molecular modelling | Receptor-ligand interactions | Vasopressin and oxytocin receptors | Molecular modelling | Vasopressin analogues | CHEMISTRY, ANALYTICAL | BIOCHEMISTRY & MOLECULAR BIOLOGY | DRUG DISCOVERY | PROTEIN-COUPLED RECEPTORS | AROMATIC RESIDUES | IDENTIFICATION | receptor-ligand interactions | ARGININE-VASOPRESSIN | HORMONE | BINDING-SITE | NEPHROGENIC DIABETES-INSIPIDUS | ANTAGONISTS | EXPRESSION | Receptors, Vasopressin - chemistry | Phenylalanine - analogs & derivatives | Phenylalanine - chemistry | Humans | Molecular Docking Simulation | Vasopressins - chemistry | Receptors, Oxytocin - chemistry
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11. Full Text Investigation of mechanism of desmopressin binding in vasopressin V2 receptor versus vasopressin V1a and oxytocin receptors: Molecular dynamics simulation of the agonist‐bound state in the membrane–aqueous system
by Ślusarz, Magdalena J and Ślusarz, Rafał and Ciarkowski, Jerzy
Biopolymers, ISSN 0006-3525, 04/2006, Volume 81, Issue 5, pp. 321 - 338
The vasopressin V2 receptor (V2R) belongs to the Class A G protein–coupled receptors (GPCRs). V2R is expressed in the renal collecting duct (CD), where it... 
GPCR | dDAVP | internal water | desmopressin | V2R | receptor activation | Desmopressin | Receptor activation | Internal water | RESIDUAL DIPOLAR COUPLINGS | TRANSMEMBRANE HELICES | CONSTITUTIVE ACTIVATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | STRUCTURAL INSTABILITY | PROTEIN-COUPLED RECEPTORS | ANTIDIURETIC ACTIVITY | PHARMACOLOGICAL PROPERTIES | ARGININE-VASOPRESSIN | BIOPHYSICS | FUNCTIONAL EXPRESSION | NEPHROGENIC DIABETES-INSIPIDUS | Water | Biopolymers - chemistry | GTP-Binding Proteins - chemistry | Peptides - chemistry | Humans | Molecular Conformation | Models, Molecular | Phosphatidylcholines - chemistry | Deamino Arginine Vasopressin - chemistry | Receptors, Oxytocin - chemistry | Amino Acid Motifs | Receptors, Vasopressin - chemistry | Computer Simulation | Deamino Arginine Vasopressin - agonists | Conserved Sequence | Protein Binding | Ligands | Protein Conformation | Cell Membrane - metabolism | Mutation | Oxytocin - chemistry
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12. Full Text Conformational stability of the full‐atom hexameric model of the ClpB chaperone from Escherichia coli
by Ziętkiewicz, Szymon and Ślusarz, Magdalena J and Ślusarz, Rafał and Liberek, Krzysztof and Rodziewicz‐Motowidło, Sylwia
Biopolymers, ISSN 0006-3525, 01/2010, Volume 93, Issue 1, pp. 47 - 60
The Escherichia coli heat shock protein ClpB, a member of the Hsp100 family, plays a crucial role in cellular thermotolerance. In co‐operation with the Hsp70... 
ClpB chaperone | M domain flexibility | conformational stability | molecular dynamics | oligomer model | Molecular dynamics | Conformational stability | Oligomer model | HSP104 | MECHANISM | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | AGGREGATED PROTEINS | DIELECTRIC MEDIUM | PROTEIN DISAGGREGATION | ATP-BINDING-SITES | SUBSTRATE-BINDING | BIOPHYSICS | N-TERMINAL DOMAIN | OLIGOMERIZATION | Endopeptidase Clp | Heat-Shock Proteins - metabolism | Adenosine Triphosphatases - metabolism | Models, Molecular | Crystallography, X-Ray | Escherichia coli Proteins - metabolism | HSP70 Heat-Shock Proteins - metabolism | Escherichia coli - metabolism | Protein Binding | Adenosine Triphosphatases - chemistry | Protein Conformation | HSP70 Heat-Shock Proteins - chemistry | Escherichia coli Proteins - chemistry | Heat-Shock Proteins - chemistry
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13. Interaction of class A G protein-coupled receptors with G proteins
by Ślusarz, Rafał and Ciarkowski, Jerzy
Acta Biochimica Polonica, ISSN 0001-527X, 2004, Volume 51, Issue 1, pp. 129 - 136
A model for interaction of class A G protein-coupled receptor with the G protein G, segment is proposed using the rhodopsin-transducin (RD/Gt) prototype. The... 
GPCR class A | Interaction | G protein | HETEROTRIMERIC G-PROTEIN | TRANSDUCIN-ALPHA | ACTIVATION | ALPHA-SUBUNIT | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | MEMBRANES | MODEL | interaction | RHODOPSIN | BINDING | METARHODOPSIN-II
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14. Full Text Use of the UNRES force field in template-assisted prediction of protein structures and the refinement of server models: Test with CASP12 targets
by Karczyńska, Agnieszka and Mozolewska, Magdalena A and Krupa, Paweł and Giełdoń, Artur and Bojarski, Krzysztof K and Zaborowski, Bartłomiej and Liwo, Adam and Ślusarz, Rafał and Ślusarz, Magdalena and Lee, Jooyoung and Joo, Keehyoung and Czaplewski, Cezary
Journal of Molecular Graphics and Modelling, ISSN 1093-3263, 08/2018, Volume 83, pp. 92 - 99
Knowledge-based methods are, at present, the most effective ones for the prediction of protein structures; however, their results heavily depend on the... 
Knowledge-based methods | Template-based restraints | Protein structure prediction | UNRES force field | Replica exchange molecular dynamics | SIDE-CHAIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOCHEMICAL RESEARCH METHODS | ALPHA | EXCHANGE MOLECULAR-DYNAMICS | CRYSTALLOGRAPHY | QUALITY ASSESSMENT | SPACE | COMPUTER SCIENCE, INTERDISCIPLINARY APPLICATIONS | MATHEMATICAL & COMPUTATIONAL BIOLOGY | BACKBONE | Proteins | Molecular dynamics | File servers | Usage | Analysis
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15. Full Text Evaluation of the scale-consistent UNRES force field in template-free prediction of protein structures in the CASP13 experiment
by Lubecka, Emilia A and Karczyńska, Agnieszka S and Lipska, Agnieszka G and Sieradzan, Adam K and Ziȩba, Karolina and Sikorska, Celina and Uciechowska, Urszula and Samsonov, Sergey A and Krupa, Paweł and Mozolewska, Magdalena A and Golon, Łukasz and Giełdoń, Artur and Czaplewski, Cezary and Ślusarz, Rafał and Ślusarz, Magdalena and Crivelli, Silvia N and Liwo, Adam
Journal of Molecular Graphics and Modelling, ISSN 1093-3263, 11/2019, Volume 92, Issue C, pp. 154 - 166
The recent NEWCT-9P version of the coarse-grained UNRES force field for proteins, with scale-consistent formulas for the local and correlation terms, has been... 
Replica-exchange molecular dynamics | Free and data-assisted modeling | protein structure prediction | Multiscale modeling | UNRES force field | TESTS | POLYPEPTIDE-CHAINS | SEARCH | BIOCHEMISTRY & MOLECULAR BIOLOGY | BIOCHEMICAL RESEARCH METHODS | CROSS-LINKING | X-RAY-SCATTERING | EXCHANGE MOLECULAR-DYNAMICS | CRYSTALLOGRAPHY | CONFORMATION | POTENTIALS | COMPUTER SCIENCE, INTERDISCIPLINARY APPLICATIONS | UNITED-RESIDUE MODEL | MATHEMATICAL & COMPUTATIONAL BIOLOGY | SIMULATIONS | Proteins | Molecular dynamics | Crosslinked polymers | Rankings | Analysis
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16. Full Text A hypothesis for GPCR activation
by Ciarkowski, Jerzy and Witt, Magdalena and Ślusarz, Rafał
Journal of Molecular Modeling, ISSN 1610-2940, 9/2005, Volume 11, Issue 4, pp. 407 - 415
Growing evidence that rhodopsin (RD) and related G protein-coupled receptors form functional dimers/oligomers, followed by direct proof (using atomic force... 
Class A | rhodopsin | Chemistry | transducin | GPCR activation | G protein | Transducin | Rhodopsin | CONTACT SITES | ALPHA-SUBUNIT | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | DIMERIZATION | ADRENERGIC-RECEPTOR | CHEMISTRY, MULTIDISCIPLINARY | 3-DIMENSIONAL STRUCTURE | COMPLEX-FORMATION | COMPUTER SCIENCE, INTERDISCIPLINARY APPLICATIONS | BIOPHYSICS | PROTEIN-COUPLED RECEPTOR | class A | COVALENT CROSS-LINKING | INVERTEBRATE RHODOPSIN |