Interplay Among Tertiary Contacts, Secondary Structure Formation and Side-chain Packing in the Protein Folding Mechanism: All-atom Representation Study of Protein L

2003 ◽  
Vol 326 (3) ◽  
pp. 933-954 ◽  
Author(s):  
Cecilia Clementi ◽  
Angel E. Garcı́a ◽  
José N. Onuchic
Keyword(s):  
Protein Folding ◽  
Secondary Structure ◽  
Structure Formation ◽  
Side Chain ◽  
Protein L ◽  
Chain Packing ◽  
Secondary Structure Formation ◽  
Folding Mechanism ◽  
Tertiary Contacts ◽  
Side Chain Packing

Peptide models of protein folding initiation sites. 1. Secondary structure formation by peptides corresponding to the G- and H-helixes of myoglobin

Biochemistry ◽  
1993 ◽  
Vol 32 (25) ◽  
pp. 6337-6347 ◽  
Author(s):  
Jonathan P. Waltho ◽  
Victoria A. Feher ◽  
Gene Merutka ◽  
H. Jane Dyson ◽  
Peter E. Wright
Keyword(s):  
Protein Folding ◽  
Secondary Structure ◽  
Structure Formation ◽  
Secondary Structure Formation ◽  
Peptide Models

Effects of Arginine Deimination and Citrulline Side‐Chain Length on Peptide Secondary Structure Formation

ChemBioChem ◽  
2019 ◽  
Vol 20 (16) ◽  
pp. 2118-2124
Author(s):  
Po‐Yi Wu ◽  
Chin‐Yi Chen ◽  
Jhe‐Hao Li ◽  
Jin‐Kai Lin ◽  
Ting‐Hsuan Chen ◽  
...  
Keyword(s):  
Secondary Structure ◽  
Structure Formation ◽  
Chain Length ◽  
Side Chain ◽  
Side Chain Length ◽  
Secondary Structure Formation ◽  
Peptide Secondary Structure

scholarly journals Main-Chain Chiral Poly(2-oxazoline)s: Influence of Alkyl Side-Chain on Secondary Structure Formation in the Solid State

2015 ◽  
Vol 350 (1) ◽  
pp. 43-54 ◽  
Author(s):  
Meta M. Bloksma ◽  
Marco M. R. M. Hendrix ◽  
Silke Rathgeber ◽  
Ulrich S. Schubert ◽  
Richard Hoogenboom
Keyword(s):  
Solid State ◽  
Secondary Structure ◽  
Structure Formation ◽  
Main Chain ◽  
Side Chain ◽  
Alkyl Side Chain ◽  
Secondary Structure Formation

Does the molten globule have a native-like tertiary fold?

1995 ◽  
Vol 348 (1323) ◽  
pp. 43-47 ◽  
Keyword(s):  
Protein Folding ◽  
Molten Globule ◽  
Side Chain ◽  
Structural Rearrangements ◽  
Chain Packing ◽  
Folding Intermediates ◽  
Final Structure ◽  
Helical Domain ◽  
Side Chain Packing

One of the mysteries in protein folding is how folding intermediates direct a protein to its unique final structure. To address this question, we have studied the molten globule formed by the α-helical domain of α-lactalbumin (α-LA) and demonstrated that it has a native-like tertiary fold, even in the absence of rigid, extensive side chain packing. These studies suggest that the role of molten globule intermediates in protein folding is to maintain an approximate native backbone topology while still allowing minor structural rearrangements to occur.

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