A combination of fluorescence blob model and molecular mechanics optimizations was applied to determine the number (Nblob) of amino acids (aa’s) located in the volume probed by an excited pyrene for poly(l-lysine) labeled with 1-pyrenebutyric acid (PyBu-PLL), as it adopted an extended conformation in DMSO. The Nblob value of PyBu-PLL was then compared to those of other pyrene-labeled polypeptides adopting a similarly extended conformation over the length scale of a blob to quantify the contribution of the pyrenyl label to Nblob. After subtracting the pyrene contribution, the plot of the corrected Nblob as a function of aa side chain reach (SCR) led to the conclusion that, for a polypeptide in an extended conformation, increasing the SCR of an aa by one bond resulted in an ∼1.8 aa increase in Nblob. This information could then be applied to predict the intrinsic Nblob value (N(SCR)) of any aa based on its SCR as long as this aa was part of an aa sequence in an extended conformation. The increase in Nblob resulting from the conformational freedom imparted by smaller aa’s to a polypeptide backbone was accounted for by multiplying N(SCR) with the bending function fb(SCS), which was determined experimentally for the different side chain sizes (SCS) of aa’s. By scanning the sequence of a protein, an Nblob value was calculated for each aa from its N(SCR) and fb(SCS) values. The Nblob values were then sorted from largest to lowest and averaged to yield ⟨Nblob⟩. Renormalization group theory was applied to determine the number (Ω) of conformations that would be available to a protein based on its ⟨Nblob⟩ value and the number of blobs found in the protein sequence. Multiplying Ω by the time required by an aa to adopt its possible conformations yielded the protein folding time (τF). A correlation coefficient of 0.73 was obtained from the comparison of the calculated and experimentally determined τF values, demonstrating the ability of this blob-based approach to predict the protein folding times within ±1.4 orders of magnitude from the experimentally determined value.