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A computational study of Neuromedin B
- Source :
- Recercat. Dipósit de la Recerca de Catalunya, instname, UPCommons. Portal del coneixement obert de la UPC, Universitat Politècnica de Catalunya (UPC)
- Publication Year :
- 2011
- Publisher :
- Elsevier BV, 2011.
-
Abstract
- A methodological study has been undertaken to assess the conformational profile of Neuromedin B (NMB) using classical molecular dynamics simulations (MD) and replica exchange molecular dynamics (REMD) simulations under generalized Born (GB) solvent conditions. Comparison of the results obtained from these simulations suggests that the peptide has a propensity to adopt both b-turns and a-helical conformations regardless of the simulation protocols used. However, the conformations adopted more helical character under REMD conditions and showed good agreement with the NMR supported structure reported in the literature.
- Subjects :
- CONFORMATIONAL-CHANGES
CELL LUNG-CANCER
THERMOREGULATION
beta-Turn
Thermodynamics
Molecular dynamics
FOLDING SIMULATIONS
Replica exchange
Biochemistry
Enginyeria química [Àrees temàtiques de la UPC]
Computational chemistry
Dinàmica molecular
Conformation
Physical and Theoretical Chemistry
NMB
AFFINITY
Chemistry
LIPID-MEMBRANES
alpha-Helical
Neuromedin B
Condensed Matter Physics
MOLECULAR-DYNAMICS SIMULATION
BOMBESIN RECEPTOR
GASTRIN-RELEASING PEPTIDE
α helical
Methodological study
Pèptids
Non small cell
Peptides
GENERALIZED BORN MODEL
Subjects
Details
- ISSN :
- 2210271X
- Volume :
- 971
- Database :
- OpenAIRE
- Journal :
- Computational and Theoretical Chemistry
- Accession number :
- edsair.doi.dedup.....f298f58352d2b4978d864ec7aeb405ad