Molecular dynamics simulation of phosphatidylcholine membrane in low ionic strengths of sodium chloride.

The one-microsecond molecular dynamics simulations of a membrane-protein complex investigate the influence of the aqueous sodium chloride solutions on the structure and dynamics of a palmitoyl-oleoyl-phosphatidylcholine bilayer membrane. The simulations were performed on five different concentrations (40, 150, 200, 300, and 400 mM) in addition to a salt-free system by using the charmm36 force field for all atoms. Four biophysical parameters, (membrane thicknesses of annular and bulk lipids, and the area per lipid of both leaflets), were computed separately.

Evaluation of the frequency and pattern of local recurrence following intersphincteric resection for ultra-low rectal cancer.

Introduction: Abdomino-perineal resection has been the standard treatment for rectal tumors located ≤5cm from the anal verge. Recently, intersphincteric resection became a valid option which preserves the bowel continuity with better functional outcome.

Aim: Is to evaluate the oncological and functional outcome alongside the associated surgical morbidity in patients with T1-3 rectal cancer, who underwent intersphincteric resection (ISR).

The use of tensor fascia lata pedicled flap in reconstructing full thickness abdominal wall defects and groin defects following tumor ablation.

Background: The tensor fascia lata is a versatile flap with many uses in reconstructive plastic surgery. As a pedicled flap its reach to the lower abdomen and groin made it an attractive option for reconstructing soft tissue defects after tumor ablation. However, debate exists on the safe dimension of the flap, as distal tip necrosis is common.

Pre-steady-state kinetic studies of the fidelity and mechanism of polymerization catalyzed by truncated human DNA polymerase lambda.

DNA polymerase lambda (Pollambda), a member of the X-family DNA polymerases, possesses an N-terminal BRCT domain, a proline-rich domain, and a C-terminal polymerase beta-like domain (tPollambda). In this paper, we determined a minimal kinetic mechanism and the fidelity of tPollambda using pre-steady-state kinetic analysis of the incorporation of a single nucleotide into a one-nucleotide gapped DNA substrate, 21-19/41-mer (primer-primer/template). Our kinetic studies revealed an incoming nucleotide bound to the enzyme.