Atomic force microscope (AFM) has become a common tool for the structural and physical studies of biological macromolecules, mainly because it provides the ability to perform experiments with samples in a buffer solution. In this study, structure of proteins and nucleic acids has been studied in their physiological environment that allows native intermolecular complexes to be formed. Cr and Au were deposited on p-Si (100) substrate by thermal evaporation method in sequence with the thickness of $200{AA}$ and $500{AA}$, respectively, since Au is adequate for immobilizing biomolecules by forming a self-assembled monolayer (SAM) with semiconductor-based biosensors. The SAM, streptavidin and biotin interacted each other with their specific binding energy and their adsorption was analyzed using the Bio-AFM both in a solution and under air environment. A silicon nitride tip was used as a contact tip of Bio-AFM measurement in a solution and an antimony doped silicon tip as a tapping tip under air environment. Actual morphology could also be obtained by 3-dimensional AFM images. The length and agglomerate size of biomolecules was measured in stages. Furthermore, $R_{a}$ (average of surface roughness) and $R_{ms}$ (mean square of surface roughness) and surface density for the adsorbed surface were also calculated from the AFM image.