Hydrophobicity of amino acid residues in globular proteins

Science ◽  
1985 ◽  
Vol 229 (4716) ◽  
pp. 834-838 ◽  
Author(s):  
G. Rose ◽  
A. Geselowitz ◽  
G. Lesser ◽  
R. Lee ◽  
M. Zehfus
Keyword(s):  
Amino Acid ◽  
Globular Proteins ◽  
Amino Acid Residues

scholarly journals The cyclol hypothesis and the “globular” proteins

1937 ◽  
Vol 161 (907) ◽  
pp. 505-524 ◽  
Keyword(s):  
Amino Acid ◽  
Hydrogen Bonds ◽  
Ad Hoc ◽  
Globular Proteins ◽  
The Body ◽  
Amino Acid Residues ◽  
Native Protein ◽  
Orderly Arrangement

A number of facts relating to proteins suggest that the polypeptides in native protein are in a folded state (Astbury 1933, 1934; Astbury and Street 1930, 1931; Pryde 1931; Wrinch 1936 a , b , c , 1937 a ; Langmuir, Schaefer and Wrinch 1937). The type of folding must be such as to imply the possibility of the regular and orderly arrangement of hundreds 01 amino-acid residues which to some extent at least is independent of the particular residues in question. We propose therefore to formulate all types of folding which are geometrically possible. Each hypothesis in turn can then be tested in two ways. We may consider its plausibility in itself: and having developed its implications to the farthest possible point, we may test it against known facts by ad hoc experiments. At present two types of folding have been suggested—by means of cyclol links (Wrinch 1936 a , b , c , 1937 a ; Langmuir, Schaefer and Wrinch 1937; Astbury 1936 a , b , c ; Frank, 1936) and by means of hydrogen bonds (Jordan Lloyd 1932; Jordan Lloyd and Marriott 1933; Mirsky and Pauling 1936; Wrinch and Jordan Lloyd 1936). The search for other types of folding is being continued. So far it has not proved possible to discard either theory on the grounds that the type of link postulated is out of the question. It is there­ fore very desirable to test these theories by means of their implications. Accordingly, on this occasion we consider (Wrinch 1937 b , c ) whether the cyclol theory can stand the test of the body of facts relating to the “globular” proteins, established by Svedberg and his collaborators (Svedberg and others 1929, 1930 a , b , 1934 a , b , 1935).

Dynamics of amino acid residues in globular proteins

2009 ◽  
Vol 24 (2) ◽  
pp. 180-191 ◽  
Author(s):  
R. BHASKARAN ◽  
P.K. PONNUSWAMY
Keyword(s):  
Amino Acid ◽  
Globular Proteins ◽  
Amino Acid Residues

scholarly journals Intrinsic Disorder-Based Design of Stable Globular Proteins

Biomolecules ◽  
2019 ◽  
Vol 10 (1) ◽  
pp. 64 ◽  
Author(s):  
Galina S. Nagibina ◽  
Ksenia A. Glukhova ◽  
Vladimir N. Uversky ◽  
Tatiana N. Melnik ◽  
Bogdan S. Melnik
Keyword(s):  
Amino Acid ◽  
Hot Spots ◽  
Point Mutations ◽  
Intrinsic Disorder ◽  
Query Protein ◽  
Globular Proteins ◽  
Amino Acid Residues ◽  
Weak Spot ◽  
Stable Mutant ◽  
Mutant Forms

Directed stabilization of globular proteins via substitution of a minimal number of amino acid residues is one of the most complicated experimental tasks. This work summarizes our research on the effect of amino acid substitutions on the protein stability utilizing the outputs of the analysis of intrinsic disorder predisposition of target proteins. This allowed us to formulate the basis of one of the possible approaches to the stabilization of globular proteins. The idea is quite simple. To stabilize a protein as a whole, one needs to find its "weakest spot" and stabilize it, but the question is how this weak spot can be found in a query protein. Our approach is based on the utilization of the computational tools for the per-residue evaluation of intrinsic disorder predisposition to search for the "weakest spot" of a query protein (i.e., the region(s) with the highest local predisposition for intrinsic disorder). When such "weakest spot" is found, it can be stabilized through a limited number of point mutations by introducing order-promoting residues at hot spots, thereby increasing structural stability of a protein as a whole. Using this approach, we were able to obtain stable mutant forms of several globular proteins, such as Gαo, GFP, ribosome protein L1, and circular permutant of apical domain of GroEL.

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