A theoretical and computational approach to ab initio structure prediction for polypeptides in water is described and applied to selected amino acid sequences for testing and preliminary validation. The method builds systematically on the extensive efforts applied to parameterization of molecular dynamics (MD) force fields, employs an empirically well-validated continuum dielectric model for solvation, and an eminently parallelizable approach to conformational search. The effective free energy of polypeptide chains is estimated from AMBER united atom potential functions, with internal degrees of freedom for both backbone and amino acid side chains explicitly treated. The hydration free energy of each structure is determined using the Generalized Born/Solvent Accessibility (GBSA) method, modified and reparameterized to include atom types consistent with the AMBER force field. The conformational search procedure employs a multiple copy, Monte Carlo simulated annealing (MCSA) protocol in full torsion angle space, applied iteratively on sets of structures of progressively lower free energy until a prediction of a structure with lowest effective free energy is obtained. Calibration tests for the effective energy function and search algorithm are performed on the alanine dipeptide, selected protein crystal structures, and united atom decoys on barnase, crambin, and six examples from the Rosetta set. Specific demonstration cases of the method are provided for the 8-mer sequence of Ala residues, a 12-residue peptide with longer side chains QLLKKLLQQLKQ, a de novo designed 16 residue peptide of sequence (AAQAA)3Y, a 15-residue sequence with a beta sheet motif, GEWTWDATKTFTVTE, and a 36 residue small protein, Villin headpiece. The Ala 8-mer readily formed an alpha-helix. An alpha-helix structure was predicted for the 16-mer, consistent with observed results from IR and CD spectroscopy and with the pattern in psi/straight phi angles of known protein structures. The predicted structure for the 12-mer, composed of a mix of helix and less regular elements of secondary structure, lies 2.65 A RMS from the observed crystal structure. Structure prediction for the 8-mer beta-motif resulted in form 4.50 A RMS from the crystal geometry. For Villin, the predicted native form is very close to the crystal structure, RMS values of 3.5 A (including sidechains), and 1.01 A (main chain only). The methodology permits a detailed analysis of the molecular forces which dominate various segments of the predicted folding trajectory. Analysis of the results in terms of internal torsional, electrostatic and van der Waals and the electrostatic and non-electrostatic contributions to hydration, including the hydrophobic effect, is presented.