Guzzo A V
Biophys J. 1965 Nov;5(6):809-22. doi: 10.1016/S0006-3495(65)86753-4.
On the basis of the known sequences and structures of myoglobin, and alpha and beta hemoglobin, a possible correlation between certain amino acids in the sequence and the location of the helical and non-helical parts of the structure is suggested. The presence in the sequence of four critical groups; proline, aspartic acid, glutamic acid, or histidine appears to be necessary (although the last three are not sufficient) for a helical disruption to form. Additional support for this correlation is obtained from analyses of proline replacement in mutant and variant proteins. A mechanism based on hydrophobic bonding is proposed as a rationale for the apparent behavior of these groups. On the basis of these rules and correlations, secondary structures can be proposed for lysozyme and tobacco mosaic virus protein which are consistent with several pieces of evidence.
基于已知的肌红蛋白、α和β血红蛋白的序列和结构，有人提出序列中的某些氨基酸与结构中螺旋和非螺旋部分的位置之间可能存在关联。序列中存在四个关键基团：脯氨酸、天冬氨酸、谷氨酸或组氨酸，似乎是形成螺旋破坏所必需的（尽管后三个并不充分）。对突变体和变体蛋白中脯氨酸替代的分析为这种关联提供了额外支持。有人提出一种基于疏水键合的机制，作为这些基团明显行为的理论依据。基于这些规则和关联，可以为溶菌酶和烟草花叶病毒蛋白提出二级结构，这与几条证据是一致的。
