01642nas a2200277 4500008004100000022001400041245015700055210006900212260010600281300001000387490000800397520061100405653002101016653001401037653001301051653001801064653001401082653001501096100002101111700002301132700001801155700002001173700001901193700002201212856013001234 2013 eng d a1386-142500aStudy of hydration of sarcosine, formation of its zwitterion and their different oligomers in aqueous media: a Raman spectroscopic and theoretical study0 aStudy of hydration of sarcosine formation of its zwitterion and  aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLANDbPERGAMON-ELSEVIER SCIENCE LTDcDEC a74-830 v1163 a

{Raman spectra of the biologically important molecule sarcosine (SAR) (C3H7NO2) were studied experimentally in aqueous solution at different concentrations. These spectra were also calculated theoretically using density functional theory (DFT) at the B3LYP/6-31 1++G(d,p) level. Further, all the observed normal modes were assigned through potential energy distribution (PED). Geometry optimization of SAR produced its three conformers with slightly different energies. The lowest energy conformer of SAR was selected for a systematic solvation study wherein different numbers of water molecules (nW

10aDFT calculations10aHydration10aOligomer10aRaman spectra10aSarcosine10aZwitterion1 aSharma, Poornima1 aSingh, Dheeraj, K.1 aGupta, Vineet1 aAsthana, B., P.1 aMishra, P., C.1 aSingh, Ranjan, K. uhttps://library.ncl.res.in/content/study-hydration-sarcosine-formation-its-zwitterion-and-their-different-oligomers-aqueous-002311nas a2200253 4500008004100000022001400041245015100055210006900206260009200275300001200367490000700379520138900386653001101775653000901786653000901795653000901804653002001813653001401833100001901847700001701866700002701883700001601910856013101926 2013 eng d a0892-702200aUnderstanding the orientation of water molecules around the phosphate and attached functional groups in a phospholipid molecule: a DFT-based study0 aUnderstanding the orientation of water molecules around the phos a4 PARK SQUARE, MILTON PARK, ABINGDON OX14 4RN, OXON, ENGLANDbTAYLOR & FRANCIS LTDcOCT a937-9550 v393 a

The adsorption of water molecules around a polar region (in particular around the phosphate moiety) in the phospholipid molecules is studied in this work. Phospholipid molecules with different functional groups are known to respond differently to the water molecules. Hence, we attempt to study the adsorption of water molecules around the phosphate group as a consequence of the change of functional group attached to the phosphate group, viz. phosphatidyl ethanolamine (PE), phosphatidyl choline (PC) and phosphatidyl glycerol (PG). As the latter is anionic in nature, the charge is compensated by Na+ counterion. Up to seven water molecules are adsorbed around the phosphate groups in model systems mimicking phospholipid molecule. The corresponding changes in the structural and electronic aspects are analysed. The significant difference between the PE and PC model systems is the formation of clathrate-like structure in the latter. Itisnoticed that as the number of water molecules increases to seven, both the hydrogen atoms in the water molecule participate in hydrogen bonding. However, in the PG model system, the charge-compensating counterion prevents the water molecule to form clathrate-like structures. The adsorption sites for water molecules are validated by density functional theory-based reactivity descriptors, viz. Fukui functions in the PE model system.

10acHelpG10aDMPC10aDMPE10aDMPG10aFukui functions10aHydration1 aMishra, Deepti1 aDas, Susanta1 aKrishnamurthy, Sailaja1 aPal, Sourav uhttps://library.ncl.res.in/content/understanding-orientation-water-molecules-around-phosphate-and-attached-functional-groups-002510nas a2200253 4500008004100000022001400041245012800055210007000183260000900253300001400262490000700276520160600283653002801889653002901917653001401946653003801960653004001998653002102038100002302059700001602082700001602098700001502114856012702129 2026 eng d a1948-719300aCombined effects of mutation and ionic strength onα-synuclein reveal generic features of aggregation-pronemonomeric states0 aCombined effects of mutation and ionic strength onαsynuclein rev cJUL  a2752-27700 v173 a

alpha-Synuclein (alpha S) is a highly charged, intrinsically disordered protein (IDP) whose aberrant aggregation is linked to Parkinson's disease (PD). Along with wild-type (WT) alpha S, five single-point mutants (A30P, E46K, H50Q, G51D, and A53T) are implicated in familial PD. To resolve contradictory experimental observations under varying solution conditions, we investigated how ionic strength modulates the relative aggregation propensity of these six monomeric alpha S variants using atomistic simulations. Structural and energetic analyses at global, domain, and residue levels revealed that aggregation propensity rankings switch with increasing ionic strength but stabilize beyond physiological concentration, while A53T and H50Q consistently remain highly aggregation-prone. We additionally identified electrostatic-driven decoupling between global and local motions. Aggregation-prone monomers preferentially populate semicompact ensembles with beta-sheet propensity, an exposed and stiff N-terminus with fewer interdomain contacts, a flexible yet compact C-terminus, and an NAC domain that is either under-protected and stiff or flexible and poorly hydrated. These monomers further exhibit strong intramolecular stabilization, poor solvation, counterion binding, and subdiffusive collapsing dynamics that may facilitate intermolecular encounters. We justified aggregation propensity trends across ionic strengths, validated physiological trends using a dimer model, suggested a generic monomer-to-aggregate mechanism, and reconciled simulations with experimental variability.

10aconformationallandscape10aelectrostatic modulation10aHydration10aintrinsically disordered proteins10amolecular flexibilityand compaction10apolymer dynamics1 aTammara, Vaishnavi1 aDas, Ankita1 aDesai, Zion1 aDas, Atanu uhttps://library.ncl.res.in/content/combined-effects-mutation-and-ionic-strength-on%CE%B1-synuclein-reveal-generic-features