simulated annealing calculations with nanoscale molecular dynamics (Molecular Dynamics Inc)
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Molecular Dynamics Inc
simulated annealing calculations with nanoscale molecular dynamics
Simulated Annealing Calculations With Nanoscale Molecular Dynamics, supplied by Molecular Dynamics Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/simulated+annealing+molecular+dynamics+calculation/simulated+annealing+calculations+with+nanoscale+molecular+dynamics/pmc09603574-206-12-13
Average 90 stars, based on 1 article reviews
Simulated Annealing Calculations With Nanoscale Molecular Dynamics, supplied by Molecular Dynamics Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/simulated+annealing+molecular+dynamics+calculation/simulated+annealing+calculations+with+nanoscale+molecular+dynamics/pmc09603574-206-12-13
Average 90 stars, based on 1 article reviews
simulated annealing calculations with nanoscale molecular dynamics - by Bioz Stars,
2026-09
90/100 stars
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Residue:Article Title: Amphipathic glycopeptides Article Snippet: .. * Residue φ ψ Conformation Thr2 62(±9) 61(±3) Random coil Gly3 −4(±2) 62(±1) Random coil Phe4 −162(±6) −52(±9) Random coil Leu5 −54(±5) −55(±7) α-helix Pro6 −61(±5) −40(±7) α-helix Asn7 −71(±3) −46(±5) α-helix Leu8 −63(±3) −34(±4) α-helix Aib9 −58(±3) −37(±3) α-helix Glu10 −82(±6) −44(±9) α-helix Lys11 −63(±3) −34(±4) α-helix Ala12 −73(±4) −33(±3) α-helix Leu13 −72(±3) −36(±3) α-helix Lys14 −73(±3) −30(±3) α-helix Ser15 −79(±8) −23(±14) α-helix Leu16 −89(±4) −59(±6) α-helix *From simulated Article Title: Glycopeptides related to beta-endorphin adopt helical amphipathic conformations in the presence of lipid bilayers. Article Snippet: A series of glycosylated endorphin analogues designed to penetrate the blood-brain barrier (BBB) have been studied by circular dichroism and by 2D-NMR in the presence of water; TFE/water; SDS micelles; and in the presence of both neutral and anionic bicelles.. In water, the glycopeptides showed only nascent helix behavior and random coil conformations.. Chemical shift indices and nuclear Overhauser effects (NOE) confirmed helices in the presence of membrane mimics. Article Title: Amphipathic glycopeptides Article Snippet: .. * Glycoeptide 9 Glycoeptide 10 Glycopeptide 11 Glycoeptide 12 Residue φ ψ φ ψ φ ψ φ ψ N-Terminal Message Segment Thr2 151(±35) −94(±9) −16(±125) −89(±)14 128(±15) 60(±6) −107(±23) −87(±59) Gly3 58(±163) 57(±7) −62(±126) −56(±4) −62(±3) −20(±5) −74(±142) −38(±64) Phe4 −122(±5) 19(±4) −81(±11) −37(±16) −88(±4) −53(±4) −69(±112) −40(±44) Leu5 −81(±3) −99(±3) −82(±17) −9(±40) −95(±48) −18(±60) 47(±56) −90(±70) C-Terminal Amphipathic Helical Address Segment Asn7/8 −148(±1) −61(±1) −46(±29) −1(±13) −74(±9) −52(±8) −129(±7) −24(±7) Leu8/9 −71(±3) −26(±2) −81(±10) −40(±5) −63(±5) −30(±10) −77(±13) −31(±4) Aib9/10 −85(±1) −24(±2) −58(±2) −33(±5) −61(±5) −54(±4) −57(±2) −32(±5) Glu10/11 −91(±2) −47(±4) −84(±5) −50(±6) −69(±5) −42(±7) −76(±10) −50(±6) Lys11/12 −58(±2) −30(±4) −60(±3) −32(±5) −63(±3) −34(±4) −61(±5) −29(±6) Ala12/13 −67(±8) −33(±4) −75(±7) −30(±4) −70(±5) −31(±4) −77(±7) −53(±5) Leu13/14 −73(±6) −33(±5) −76(±6) −52(±4) −75(±4) −51(±3) −66(±3) −26(±6) Lys14/15 −76(±6) −32(±5) −64(±2) −28(±4) −64(±2) −42(±3) −76(±6) −32(±6) Ser15/16 −89(±18) −32(±32) −81(±11) −24(±18) −67(±3) −27(±4) −88(±14) −50(±17) Leu16/17 −85(±6) −57(±18) −87(±6) −58(±7) 88(±3) −60(±1) −112(±19) −73(±69) *The average backbone torsion angles from simulated Glycoproteomics:Article Title: Glycopeptides related to beta-endorphin adopt helical amphipathic conformations in the presence of lipid bilayers. Article Snippet: A series of glycosylated endorphin analogues designed to penetrate the blood-brain barrier (BBB) have been studied by circular dichroism and by 2D-NMR in the presence of water; TFE/water; SDS micelles; and in the presence of both neutral and anionic bicelles.. In water, the glycopeptides showed only nascent helix behavior and random coil conformations.. Chemical shift indices and nuclear Overhauser effects (NOE) confirmed helices in the presence of membrane mimics. Article Title: Amphipathic glycopeptides Article Snippet: .. * Glycoeptide 9 Glycoeptide 10 Glycopeptide 11 Glycoeptide 12 Residue φ ψ φ ψ φ ψ φ ψ N-Terminal Message Segment Thr2 151(±35) −94(±9) −16(±125) −89(±)14 128(±15) 60(±6) −107(±23) −87(±59) Gly3 58(±163) 57(±7) −62(±126) −56(±4) −62(±3) −20(±5) −74(±142) −38(±64) Phe4 −122(±5) 19(±4) −81(±11) −37(±16) −88(±4) −53(±4) −69(±112) −40(±44) Leu5 −81(±3) −99(±3) −82(±17) −9(±40) −95(±48) −18(±60) 47(±56) −90(±70) C-Terminal Amphipathic Helical Address Segment Asn7/8 −148(±1) −61(±1) −46(±29) −1(±13) −74(±9) −52(±8) −129(±7) −24(±7) Leu8/9 −71(±3) −26(±2) −81(±10) −40(±5) −63(±5) −30(±10) −77(±13) −31(±4) Aib9/10 −85(±1) −24(±2) −58(±2) −33(±5) −61(±5) −54(±4) −57(±2) −32(±5) Glu10/11 −91(±2) −47(±4) −84(±5) −50(±6) −69(±5) −42(±7) −76(±10) −50(±6) Lys11/12 −58(±2) −30(±4) −60(±3) −32(±5) −63(±3) −34(±4) −61(±5) −29(±6) Ala12/13 −67(±8) −33(±4) −75(±7) −30(±4) −70(±5) −31(±4) −77(±7) −53(±5) Leu13/14 −73(±6) −33(±5) −76(±6) −52(±4) −75(±4) −51(±3) −66(±3) −26(±6) Lys14/15 −76(±6) −32(±5) −64(±2) −28(±4) −64(±2) −42(±3) −76(±6) −32(±6) Ser15/16 −89(±18) −32(±32) −81(±11) −24(±18) −67(±3) −27(±4) −88(±14) −50(±17) Leu16/17 −85(±6) −57(±18) −87(±6) −58(±7) 88(±3) −60(±1) −112(±19) −73(±69) *The average backbone torsion angles from simulated |