The protein molecule in solution is a beautiful but complex world by itself. Weak forces of interatomic interactions, structural organization within, and varieties of relaxation dynamics offer a plethora of problems. Equally puzzling is the act of structure acquisition starting from the nascent polypeptide chain. We study these problems using NMR spectroscopy, stopped-flow and laser-based kinetics, and computer modeling and analyses. Currently, we are at the verge of completing the NMR solution structure of Arabidopsis thaliana Phloem Protein 16 (AtPP16), which putatively delivers mRNA in plants. Other ongoing work includes equilibrium thermodynamics and kinetics of protein folding, internal friction in proteins, structure and enzymic function of eukaryotic ribosomal protein S4, and intraprotein energy dissipation response to an impulse.