Turns in Peptides and Proteins

Gd, Rose; Lm, Gierasch; Ja, Smith

doi:10.1016/s0065-3233(08)60063-7

Cited by 1,728 publications

(1,199 citation statements)

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“…&Turns are a common element of protein secondary structure and constitute about one-quarter of the residues in typical globular proteins (Wilmot & Thornton, 1988) herent polar nature of most &turns is such that they are generally situated on the surface of proteins. The surface exposure of &turns and their preference for residues bearing polar side chains such as Asn, Asp, Ser, Thr, and Arg (Rose et al, 1985) has led to speculation about their role as sites for molecular recognition, and this has been supported by considerable experimental evidence (for a review, see Rose et al [1985]). In cases where &turns do constitute a site for molecular recognition, it is likely that the precise nature of the side chain functionalities and their spatial orientation will be of critical importance.…”

Section: Discussionmentioning

confidence: 99%

Structural engineering of the HIV‐1 protease molecule with a β‐turn mimic of fixed geometry

1993

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An important goal in the de novo design of enzymes is the control of molecular geometry. To this end, an analog of the protease from human immunodeficiency virus 1 (HIV-1 protease) was prepared by total chemical synthesis, containing a constrained, nonpeptidic type 11' 0-turn mimic of predetermined three-dimensional structure.The mimic &turn replaced residues GlyI6,l7 in each subunit of the homodimeric molecule. These residues constitute the central amino acids of two symmetry-related type I' 0-turns in the native, unliganded enzyme. The 0-turn mimic-containing enzyme analog was fully active, possessed the same substrate specificity as the GlyI67l7-containing enzyme, and showed enhanced resistance to thermal inactivation. These results indicate that the precise geometry of the @turn at residues 15-18 in each subunit is not critical for activity, and that replacement of the native sequence with a rigid 0-turn mimic can lead to enhanced protein stability. Finally, the successful incorporation of a fixed element of secondary structure illustrates the potential of a "molecular kit set" approach to protein design and synthesis.

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Section: Discussionmentioning

confidence: 99%

Structural engineering of the HIV‐1 protease molecule with a β‐turn mimic of fixed geometry

1993

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“…Furthermore, Pro is an amino acid with a marked preference for the i 1 1 corner position of either type-I or type-II b-turn. 10,11 A Pro residue internal to a peptide sequence cannot offer the classical H-bonding donor NÀ ÀH group for helix stabilization. It is for this reason that Pro residues are normally found near the N-terminus of peptide helices.…”

Section: Introductionmentioning

confidence: 99%

C^α‐Methyl proline: A unique example of split personality

et al. 2007

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Methylation at the Cα‐position of a Pro residue was expected to lock the preceding tertiary amide (ω) torsion angle of the resulting (αMe)Pro to the trans disposition and to restrict the ϕ,ψ surface to the single region where the 310/α‐helices are found (in this five‐membered ring residue ϕ is severely constrained to about ±65° by its cyclic nature). The results of the present X‐ray diffraction work on a selected set of four Nα‐blocked, (αMe)Pro‐containing, dipeptide N′‐alkylamides clearly show that, although the region of the conformational map largely preferred by (αMe)Pro would indeed be that typical of 310/α‐helices, the semi‐extended [type‐II poly(Pro)n helix] region can also be explored by this extremely sterically demanding Cα‐tetrasubstituted α‐amino acid. In addition, the known high propensity for β‐turn formation of the Pro residue is further enhanced in peptides based on its Cα‐methylated derivative. © 2007 Wiley Periodicals, Inc. Biopolymers 89: 465–470, 2008.This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com

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“…The n ? 3 type hydrogen bonds characterize the b turns, which may be either homochiral or heterochiral depending on the stereochemistry of its central two residues (Rose et al 1985). Trains of consecutive n ?…”

Section: Chirality Defining Secondary Structure Of a Polypeptidementioning

confidence: 99%